---
APC_amount: 4215,38 EUR
DOAJ_listed: '1'
OA_place: publisher
OA_type: gold
PlanS_conform: '1'
_id: '19963'
abstract:
- lang: eng
text: The acquisition of cellular identity requires large-scale alterations in cellular
state. The noncanonical proteasome activator PSME3 is known to regulate diverse
cellular processes, but its importance for differentiation remains unclear. Here,
we demonstrate that PSME3 binds dynamically to highly active promoters over the
course of differentiation. However, loss of PSME3 does not globally affect mRNA
transcription. We find instead that PSME3 influences the levels of several adhesion-related
proteins and acts upstream of the HSP90 co-chaperone NUDC to regulate cell motility
and myoblast differentiation in a proteasome-independent manner. Our findings
reveal several new facets of PSME3 functionality and highlight its importance
for the differentiation of myogenic cells.
acknowledged_ssus:
- _id: LifeSc
- _id: Bio
acknowledgement: 'All proteomics analysis was done by the ISTA LSF Mass Spectrometry
Service: Ewelina Dutkiewicz-Kopczynska processed the samples (digest and cleanup);
Bella Bruszel optimized the acquisition methods, acquired the data, and performed
all searches; and Armel Nicolas provided pre- and post-project consulting and post-processed
the search results using a development version of their data analysis package, proteoCraft
(publication pending). The authors would like to thank Saki for their clarity of
thought and insight, as well as Dr. Lorenzo Puri and the members of his laboratory
for invaluable discussions relating to the project. This research was further supported
by the Lab Support Facility and the Imaging and Optics Facility of ISTA.'
article_number: e202503208
article_processing_charge: Yes
article_type: original
author:
- first_name: Kenneth D
full_name: Kuhn, Kenneth D
id: 7deed7e0-0133-11f0-8590-c4600b08d0f4
last_name: Kuhn
- first_name: Ukrae H.
full_name: Cho, Ukrae H.
last_name: Cho
- first_name: Martin W
full_name: Hetzer, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: Hetzer
orcid: 0000-0002-2111-992X
citation:
ama: Kuhn KD, Cho UH, Hetzer M. PSME3 regulates migration and differentiation of
myoblasts. Life Science Alliance. 2025;8(9). doi:10.26508/lsa.202503208
apa: Kuhn, K. D., Cho, U. H., & Hetzer, M. (2025). PSME3 regulates migration
and differentiation of myoblasts. Life Science Alliance. Embo Press. https://doi.org/10.26508/lsa.202503208
chicago: Kuhn, Kenneth D, Ukrae H. Cho, and Martin Hetzer. “PSME3 Regulates Migration
and Differentiation of Myoblasts.” Life Science Alliance. Embo Press, 2025.
https://doi.org/10.26508/lsa.202503208.
ieee: K. D. Kuhn, U. H. Cho, and M. Hetzer, “PSME3 regulates migration and differentiation
of myoblasts,” Life Science Alliance, vol. 8, no. 9. Embo Press, 2025.
ista: Kuhn KD, Cho UH, Hetzer M. 2025. PSME3 regulates migration and differentiation
of myoblasts. Life Science Alliance. 8(9), e202503208.
mla: Kuhn, Kenneth D., et al. “PSME3 Regulates Migration and Differentiation of
Myoblasts.” Life Science Alliance, vol. 8, no. 9, e202503208, Embo Press,
2025, doi:10.26508/lsa.202503208.
short: K.D. Kuhn, U.H. Cho, M. Hetzer, Life Science Alliance 8 (2025).
corr_author: '1'
date_created: 2025-07-06T22:01:22Z
date_published: 2025-09-01T00:00:00Z
date_updated: 2026-05-20T08:38:04Z
day: '01'
ddc:
- '570'
department:
- _id: MaHe
doi: 10.26508/lsa.202503208
external_id:
isi:
- '001511452100001'
pmid:
- '40537284'
file:
- access_level: open_access
checksum: 591d47aa39fc969986c7d3b966890f5f
content_type: application/pdf
creator: dernst
date_created: 2025-12-30T09:17:09Z
date_updated: 2025-12-30T09:17:09Z
file_id: '20904'
file_name: 2025_LifeScienceAlliance_Kuhn.pdf
file_size: 5471288
relation: main_file
success: 1
file_date_updated: 2025-12-30T09:17:09Z
has_accepted_license: '1'
intvolume: ' 8'
isi: 1
issue: '9'
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: B67AFEDC-15C9-11EA-A837-991A96BB2854
name: IST Austria Open Access Fund
publication: Life Science Alliance
publication_identifier:
eissn:
- 2575-1077
publication_status: published
publisher: Embo Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: PSME3 regulates migration and differentiation of myoblasts
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 8
year: '2025'
...
---
OA_place: publisher
OA_type: hybrid
PlanS_conform: '1'
_id: '20154'
abstract:
- lang: eng
text: In long-lived mammals, including humans, brain cell homeostasis is critical
for maintaining brain function throughout life. Most neurons are generated during
development and must maintain their cellular identity and plasticity to preserve
brain function. Although extensive studies indicate the importance of recycling
and regenerating cellular molecules to maintain cellular homeostasis, recent evidence
has shown that some proteins and RNAs do not turn over for months and even years.
We propose that these long-lived cellular molecules may be the basis for maintaining
brain function in the long term, but also a potential convergent target of brain
aging. We highlight key discoveries and challenges, and propose potential directions
to unravel the mystery of brain cell longevity.
acknowledgement: The work was supported by the Deutsche Forschungsgemeinschaft (DFG,
German Research Foundation) (470322152 – T1347/3-1; 497658532 – T1347/4-1; 507965872
– T1347/5-1; and 460333672 – CRC1540 Exploring Brain Mechanics) to T.T., the Schram
Foundation (T.T.), the European Research Council (ERC-2018-STG, 804468 EAGER; ERC-2023-COG,
101125034 NEUTIME) to T.T., the Hans-Georg Geis und Xue Hong Dong-Geis Foundation
and Forschungsstiftung Medizin am Universitätsklinikum Erlangen to T.T., and the
Interdisciplinary Centre for Clinical Research Erlangen (Interdisziplinäres Zentrum
für Klinische Forschung, Universitätsklinikum Erlangen; P162 to T.T.). We thank
Dr Laura J. Harrison for editing assistance.
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Martin W
full_name: Hetzer, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: Hetzer
orcid: 0000-0002-2111-992X
- first_name: Tomohisa
full_name: Toda, Tomohisa
last_name: Toda
citation:
ama: Hetzer M, Toda T. Long-lived cellular molecules in the brain. Trends in
Neurosciences. 2025;48(9):645-654. doi:10.1016/j.tins.2025.07.004
apa: Hetzer, M., & Toda, T. (2025). Long-lived cellular molecules in the brain.
Trends in Neurosciences. Elsevier. https://doi.org/10.1016/j.tins.2025.07.004
chicago: Hetzer, Martin, and Tomohisa Toda. “Long-Lived Cellular Molecules in the
Brain.” Trends in Neurosciences. Elsevier, 2025. https://doi.org/10.1016/j.tins.2025.07.004.
ieee: M. Hetzer and T. Toda, “Long-lived cellular molecules in the brain,” Trends
in Neurosciences, vol. 48, no. 9. Elsevier, pp. 645–654, 2025.
ista: Hetzer M, Toda T. 2025. Long-lived cellular molecules in the brain. Trends
in Neurosciences. 48(9), 645–654.
mla: Hetzer, Martin, and Tomohisa Toda. “Long-Lived Cellular Molecules in the Brain.”
Trends in Neurosciences, vol. 48, no. 9, Elsevier, 2025, pp. 645–54, doi:10.1016/j.tins.2025.07.004.
short: M. Hetzer, T. Toda, Trends in Neurosciences 48 (2025) 645–654.
corr_author: '1'
date_created: 2025-08-10T22:01:29Z
date_published: 2025-09-01T00:00:00Z
date_updated: 2025-12-29T13:47:58Z
day: '01'
ddc:
- '570'
department:
- _id: MaHe
doi: 10.1016/j.tins.2025.07.004
external_id:
isi:
- '001568965400001'
pmid:
- '40744775'
file:
- access_level: open_access
checksum: 90942491b499f70b0bf48b8aec2e7387
content_type: application/pdf
creator: dernst
date_created: 2025-12-29T13:47:27Z
date_updated: 2025-12-29T13:47:27Z
file_id: '20873'
file_name: 2025_TrendsNeurosciences_Hetzer.pdf
file_size: 327847
relation: main_file
success: 1
file_date_updated: 2025-12-29T13:47:27Z
has_accepted_license: '1'
intvolume: ' 48'
isi: 1
issue: '9'
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
page: 645-654
pmid: 1
publication: Trends in Neurosciences
publication_identifier:
eissn:
- 1878-108X
issn:
- 0166-2236
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Long-lived cellular molecules in the brain
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 48
year: '2025'
...
---
OA_place: repository
OA_type: green
_id: '15316'
abstract:
- lang: eng
text: Genomic DNA that resides in the nuclei of mammalian neurons can be as old
as the organism itself. The life span of nuclear RNAs, which are critical for
proper chromatin architecture and transcription regulation, has not been determined
in adult tissues. In this work, we identified and characterized nuclear RNAs that
do not turn over for at least 2 years in a subset of postnatally born cells in
the mouse brain. These long-lived RNAs were stably retained in nuclei in a neural
cell type–specific manner and were required for the maintenance of heterochromatin.
Thus, the life span of neural cells may depend on both the molecular longevity
of DNA for the storage of genetic information and also the extreme stability of
RNA for the functional organization of chromatin.
acknowledgement: 'European Research Council: ERC-2018-STG, 804468 EAGER; European
Research Council: ERC-2023-COG, 101125034 NEUTIME; Deutsche Forschungsgemeinschaft:
TO1347/4-1; Boehringer Ingelheim Stiftung; Deutsches Zentrum für Neurodegenerative
Erkrankungen'
article_processing_charge: No
article_type: original
author:
- first_name: Sara
full_name: Zocher, Sara
last_name: Zocher
- first_name: Asako
full_name: Mccloskey, Asako
last_name: Mccloskey
- first_name: Anne
full_name: Karasinsky, Anne
last_name: Karasinsky
- first_name: Roberta
full_name: Schulte, Roberta
last_name: Schulte
- first_name: Ulrike
full_name: Friedrich, Ulrike
last_name: Friedrich
- first_name: Mathias
full_name: Lesche, Mathias
last_name: Lesche
- first_name: Nicole
full_name: Rund, Nicole
last_name: Rund
- first_name: Fred H.
full_name: Gage, Fred H.
last_name: Gage
- first_name: Martin W
full_name: Hetzer, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: Hetzer
orcid: 0000-0002-2111-992X
- first_name: Tomohisa
full_name: Toda, Tomohisa
last_name: Toda
citation:
ama: Zocher S, Mccloskey A, Karasinsky A, et al. Lifelong persistence of nuclear
RNAs in the mouse brain. Science. 2024;384(6691):53-59. doi:10.1126/science.adf3481
apa: Zocher, S., Mccloskey, A., Karasinsky, A., Schulte, R., Friedrich, U., Lesche,
M., … Toda, T. (2024). Lifelong persistence of nuclear RNAs in the mouse brain.
Science. AAAS. https://doi.org/10.1126/science.adf3481
chicago: Zocher, Sara, Asako Mccloskey, Anne Karasinsky, Roberta Schulte, Ulrike
Friedrich, Mathias Lesche, Nicole Rund, Fred H. Gage, Martin Hetzer, and Tomohisa
Toda. “Lifelong Persistence of Nuclear RNAs in the Mouse Brain.” Science.
AAAS, 2024. https://doi.org/10.1126/science.adf3481.
ieee: S. Zocher et al., “Lifelong persistence of nuclear RNAs in the mouse
brain,” Science, vol. 384, no. 6691. AAAS, pp. 53–59, 2024.
ista: Zocher S, Mccloskey A, Karasinsky A, Schulte R, Friedrich U, Lesche M, Rund
N, Gage FH, Hetzer M, Toda T. 2024. Lifelong persistence of nuclear RNAs in the
mouse brain. Science. 384(6691), 53–59.
mla: Zocher, Sara, et al. “Lifelong Persistence of Nuclear RNAs in the Mouse Brain.”
Science, vol. 384, no. 6691, AAAS, 2024, pp. 53–59, doi:10.1126/science.adf3481.
short: S. Zocher, A. Mccloskey, A. Karasinsky, R. Schulte, U. Friedrich, M. Lesche,
N. Rund, F.H. Gage, M. Hetzer, T. Toda, Science 384 (2024) 53–59.
corr_author: '1'
date_created: 2024-04-14T22:01:01Z
date_published: 2024-04-04T00:00:00Z
date_updated: 2025-09-04T13:39:58Z
day: '04'
department:
- _id: MaHe
doi: 10.1126/science.adf3481
external_id:
isi:
- '001253335100031'
pmid:
- '38574132'
intvolume: ' 384'
isi: 1
issue: '6691'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7615865
month: '04'
oa: 1
oa_version: Submitted Version
page: 53-59
pmid: 1
publication: Science
publication_identifier:
eissn:
- 1095-9203
issn:
- 0036-8075
publication_status: published
publisher: AAAS
quality_controlled: '1'
related_material:
link:
- description: News on ISTA website
relation: press_release
url: https://ista.ac.at/en/news/nerve-cells-old-at-heart/
scopus_import: '1'
status: public
title: Lifelong persistence of nuclear RNAs in the mouse brain
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 384
year: '2024'
...
---
DOAJ_listed: '1'
OA_place: publisher
OA_type: gold
_id: '18480'
abstract:
- lang: eng
text: Caloric restriction (CR) can extend the organism life- and health-span by
improving glucose homeostasis. How CR affects the structure-function of pancreatic
beta cells remains unknown. We used single nucleus transcriptomics to show that
CR increases the expression of genes for beta cell identity, protein processing,
and organelle homeostasis. Gene regulatory network analysis reveal that CR activates
transcription factors important for beta cell identity and homeostasis, while
imaging metabolomics demonstrates that beta cells upon CR are more energetically
competent. In fact, high-resolution microscopy show that CR reduces beta cell
mitophagy to increase mitochondria mass and the potential for ATP generation.
However, CR beta cells have impaired adaptive proliferation in response to high
fat diet feeding. Finally, we show that long-term CR delays the onset of beta
cell aging hallmarks and promotes cell longevity by reducing beta cell turnover.
Therefore, CR could be a feasible approach to preserve compromised beta cell structure-function
during aging and diabetes.
acknowledgement: We are thankful to Michelle Reyzer from the Vanderbilt Mass Spectrometry
Research Center for assistance with MALDI-MS imaging and analysis, to the outstanding
team at the Vanderbilt Mouse Metabolic Phenotyping Center for all the assistance
with in vivo glucose homeostasis tests (DK135073, 1S10RR028101-01). We also thank
the University of Michigan Animal Phenotyping Core for conducting the bomb calorimetry
experiments (1U2CDK110768, DK020575, and DK089503). This research was supported
by recruitment funds from the Vanderbilt’s Department of Molecular Physiology and
Biophysics and NIH grants 1R03DK127484, 5U24DK097771, and 1R01DK138141 to RAeD,
by a grant from the Canadian Institutes of Health Research (CIHR; 487188) to PEM,
by and NIH DK132669 to D.D. PEM holds the Canada Research Chair in Islet Biology.
article_number: '9063'
article_processing_charge: Yes
article_type: original
author:
- first_name: Cristiane
full_name: Dos Santos, Cristiane
last_name: Dos Santos
- first_name: Amanda
full_name: Cambraia, Amanda
last_name: Cambraia
- first_name: Shristi
full_name: Shrestha, Shristi
last_name: Shrestha
- first_name: Melanie
full_name: Cutler, Melanie
last_name: Cutler
- first_name: Matthew
full_name: Cottam, Matthew
last_name: Cottam
- first_name: Guy
full_name: Perkins, Guy
last_name: Perkins
- first_name: Varda
full_name: Lev-Ram, Varda
last_name: Lev-Ram
- first_name: Birbickram
full_name: Roy, Birbickram
last_name: Roy
- first_name: Christopher
full_name: Acree, Christopher
last_name: Acree
- first_name: Keun Young
full_name: Kim, Keun Young
last_name: Kim
- first_name: Thomas
full_name: Deerinck, Thomas
last_name: Deerinck
- first_name: Danielle
full_name: Dean, Danielle
last_name: Dean
- first_name: Jean Philippe
full_name: Cartailler, Jean Philippe
last_name: Cartailler
- first_name: Patrick E.
full_name: Macdonald, Patrick E.
last_name: Macdonald
- first_name: Martin W
full_name: Hetzer, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: Hetzer
orcid: 0000-0002-2111-992X
- first_name: Mark
full_name: Ellisman, Mark
last_name: Ellisman
- first_name: Rafael
full_name: Arrojo E Drigo, Rafael
last_name: Arrojo E Drigo
citation:
ama: Dos Santos C, Cambraia A, Shrestha S, et al. Calorie restriction increases
insulin sensitivity to promote beta cell homeostasis and longevity in mice. Nature
Communications. 2024;15. doi:10.1038/s41467-024-53127-2
apa: Dos Santos, C., Cambraia, A., Shrestha, S., Cutler, M., Cottam, M., Perkins,
G., … Arrojo E Drigo, R. (2024). Calorie restriction increases insulin sensitivity
to promote beta cell homeostasis and longevity in mice. Nature Communications.
Springer Nature. https://doi.org/10.1038/s41467-024-53127-2
chicago: Dos Santos, Cristiane, Amanda Cambraia, Shristi Shrestha, Melanie Cutler,
Matthew Cottam, Guy Perkins, Varda Lev-Ram, et al. “Calorie Restriction Increases
Insulin Sensitivity to Promote Beta Cell Homeostasis and Longevity in Mice.” Nature
Communications. Springer Nature, 2024. https://doi.org/10.1038/s41467-024-53127-2.
ieee: C. Dos Santos et al., “Calorie restriction increases insulin sensitivity
to promote beta cell homeostasis and longevity in mice,” Nature Communications,
vol. 15. Springer Nature, 2024.
ista: Dos Santos C, Cambraia A, Shrestha S, Cutler M, Cottam M, Perkins G, Lev-Ram
V, Roy B, Acree C, Kim KY, Deerinck T, Dean D, Cartailler JP, Macdonald PE, Hetzer
M, Ellisman M, Arrojo E Drigo R. 2024. Calorie restriction increases insulin sensitivity
to promote beta cell homeostasis and longevity in mice. Nature Communications.
15, 9063.
mla: Dos Santos, Cristiane, et al. “Calorie Restriction Increases Insulin Sensitivity
to Promote Beta Cell Homeostasis and Longevity in Mice.” Nature Communications,
vol. 15, 9063, Springer Nature, 2024, doi:10.1038/s41467-024-53127-2.
short: C. Dos Santos, A. Cambraia, S. Shrestha, M. Cutler, M. Cottam, G. Perkins,
V. Lev-Ram, B. Roy, C. Acree, K.Y. Kim, T. Deerinck, D. Dean, J.P. Cartailler,
P.E. Macdonald, M. Hetzer, M. Ellisman, R. Arrojo E Drigo, Nature Communications
15 (2024).
date_created: 2024-10-27T23:01:44Z
date_published: 2024-10-21T00:00:00Z
date_updated: 2025-09-08T14:32:38Z
day: '21'
ddc:
- '570'
department:
- _id: MaHe
doi: 10.1038/s41467-024-53127-2
external_id:
isi:
- '001426270600023'
pmid:
- '39433757'
file:
- access_level: open_access
checksum: b936b1c047f41cd427f00e3dc79327d3
content_type: application/pdf
creator: dernst
date_created: 2024-11-04T10:37:56Z
date_updated: 2024-11-04T10:37:56Z
file_id: '18502'
file_name: 2024_NatureComm_dosSantos.pdf
file_size: 7358742
relation: main_file
success: 1
file_date_updated: 2024-11-04T10:37:56Z
has_accepted_license: '1'
intvolume: ' 15'
isi: 1
language:
- iso: eng
month: '10'
oa: 1
oa_version: Published Version
pmid: 1
publication: Nature Communications
publication_identifier:
eissn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Calorie restriction increases insulin sensitivity to promote beta cell homeostasis
and longevity in mice
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 15
year: '2024'
...
---
_id: '12880'
abstract:
- lang: eng
text: Peripheral heterochromatin positioning depends on nuclear envelope associated
proteins and repressive histone modifications. Here we show that overexpression
(OE) of Lamin B1 (LmnB1) leads to the redistribution of peripheral heterochromatin
into heterochromatic foci within the nucleoplasm. These changes represent a perturbation
of heterochromatin binding at the nuclear periphery (NP) through a mechanism independent
from altering other heterochromatin anchors or histone post-translational modifications.
We further show that LmnB1 OE alters gene expression. These changes do not correlate
with different levels of H3K9me3, but a significant number of the misregulated
genes were likely mislocalized away from the NP upon LmnB1 OE. We also observed
an enrichment of developmental processes amongst the upregulated genes. ~74% of
these genes were normally repressed in our cell type, suggesting that LmnB1 OE
promotes gene de-repression. This demonstrates a broader consequence of LmnB1
OE on cell fate, and highlights the importance of maintaining proper levels of
LmnB1.
acknowledgement: 'We thank members of the Hetzer lab for critical review of the manuscript;
Novogene for mRNA library preparation and sequencing; the Next-Generation Sequencing
Core Facility at the Salk Institute, with funding from NIH-NCI CCSG: P30 014195,
the Chapman Foundation, and the Helmsley Charitable Trust, for sequencing Cut&Run
libraries; and the Waitt Advanced Biophotonics Core Facility at the Salk Institute,
with funding from NIH-NCI CCSG: P30 014195, the Waitt Foundation, and the Chan-Zuckerberg
Initiative Imaging Scientist Award, for electron microscopy sample preparation and
imaging.'
article_number: '2202548'
article_processing_charge: No
article_type: original
author:
- first_name: Jeanae M.
full_name: Kaneshiro, Jeanae M.
last_name: Kaneshiro
- first_name: Juliana S.
full_name: Capitanio, Juliana S.
last_name: Capitanio
- first_name: Martin W
full_name: Hetzer, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: Hetzer
orcid: 0000-0002-2111-992X
citation:
ama: Kaneshiro JM, Capitanio JS, Hetzer M. Lamin B1 overexpression alters chromatin
organization and gene expression. Nucleus. 2023;14(1). doi:10.1080/19491034.2023.2202548
apa: Kaneshiro, J. M., Capitanio, J. S., & Hetzer, M. (2023). Lamin B1 overexpression
alters chromatin organization and gene expression. Nucleus. Taylor &
Francis. https://doi.org/10.1080/19491034.2023.2202548
chicago: Kaneshiro, Jeanae M., Juliana S. Capitanio, and Martin Hetzer. “Lamin B1
Overexpression Alters Chromatin Organization and Gene Expression.” Nucleus.
Taylor & Francis, 2023. https://doi.org/10.1080/19491034.2023.2202548.
ieee: J. M. Kaneshiro, J. S. Capitanio, and M. Hetzer, “Lamin B1 overexpression
alters chromatin organization and gene expression,” Nucleus, vol. 14, no.
1. Taylor & Francis, 2023.
ista: Kaneshiro JM, Capitanio JS, Hetzer M. 2023. Lamin B1 overexpression alters
chromatin organization and gene expression. Nucleus. 14(1), 2202548.
mla: Kaneshiro, Jeanae M., et al. “Lamin B1 Overexpression Alters Chromatin Organization
and Gene Expression.” Nucleus, vol. 14, no. 1, 2202548, Taylor & Francis,
2023, doi:10.1080/19491034.2023.2202548.
short: J.M. Kaneshiro, J.S. Capitanio, M. Hetzer, Nucleus 14 (2023).
corr_author: '1'
date_created: 2023-04-30T22:01:06Z
date_published: 2023-04-18T00:00:00Z
date_updated: 2024-10-09T21:05:01Z
day: '18'
ddc:
- '570'
department:
- _id: MaHe
doi: 10.1080/19491034.2023.2202548
external_id:
isi:
- '000971629400001'
pmid:
- '37071033'
file:
- access_level: open_access
checksum: 8e707eda84f64dbad7f03545ae0a83ef
content_type: application/pdf
creator: dernst
date_created: 2023-05-02T07:24:55Z
date_updated: 2023-05-02T07:24:55Z
file_id: '12884'
file_name: 2023_Nucleus_Kaneshiro.pdf
file_size: 3811113
relation: main_file
success: 1
file_date_updated: 2023-05-02T07:24:55Z
has_accepted_license: '1'
intvolume: ' 14'
isi: 1
issue: '1'
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc/4.0/
month: '04'
oa: 1
oa_version: Published Version
pmid: 1
publication: Nucleus
publication_identifier:
eissn:
- 1949-1042
issn:
- 1949-1034
publication_status: published
publisher: Taylor & Francis
quality_controlled: '1'
scopus_import: '1'
status: public
title: Lamin B1 overexpression alters chromatin organization and gene expression
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode
name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
short: CC BY-NC (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 14
year: '2023'
...
---
_id: '14315'
abstract:
- lang: eng
text: During apoptosis, caspases degrade 8 out of ~30 nucleoporins to irreversibly
demolish the nuclear pore complex. However, for poorly understood reasons, caspases
are also activated during cell differentiation. Here, we show that sublethal activation
of caspases during myogenesis results in the transient proteolysis of four peripheral
Nups and one transmembrane Nup. ‘Trimmed’ NPCs become nuclear export-defective,
and we identified in an unbiased manner several classes of cytoplasmic, plasma
membrane, and mitochondrial proteins that rapidly accumulate in the nucleus. NPC
trimming by non-apoptotic caspases was also observed in neurogenesis and endoplasmic
reticulum stress. Our results suggest that caspases can reversibly modulate nuclear
transport activity, which allows them to function as agents of cell differentiation
and adaptation at sublethal levels.
acknowledgement: 'We thank the members of the Hetzer laboratory, Tony Hunter (Salk),
Lorenzo Puri (Sanford Burnham Prebys), and Jongmin Kim (Massachusetts General Hospital)
for the critical reading of the manuscript; Kenneth Diffenderfer and Aimee Pankonin
(Stem Cell Core at the Salk Institute) for help with neurogenesis; Carol Marchetto
and Fred Gage (Salk) for providing H9 embryonic stem cells; Lorenzo Puri, Alexandra
Sacco, and Luca Caputo (Sanford Burnham Prebys) for helpful discussions and sharing
mouse primary myoblasts. This work was supported by a Glenn Foundation for Medical
Research Postdoctoral Fellowship in Aging Research (UHC), the NOMIS foundation (MWH),
and the National Institutes of Health (R01 NS096786 to MWH and K01 AR080828 to UHC).
This work was also supported by the Mass Spectrometry Core of the Salk Institute
with funding from NIH-NCI CCSG: P30 014195 and the Helmsley Center for Genomic Medicine.
We thank Jolene Diedrich and Antonio Pinto for technical support.'
article_number: RP89066
article_processing_charge: Yes
article_type: original
author:
- first_name: Ukrae H.
full_name: Cho, Ukrae H.
last_name: Cho
- first_name: Martin W
full_name: Hetzer, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: Hetzer
orcid: 0000-0002-2111-992X
citation:
ama: Cho UH, Hetzer M. Caspase-mediated nuclear pore complex trimming in cell differentiation
and endoplasmic reticulum stress. eLife. 2023;12. doi:10.7554/eLife.89066
apa: Cho, U. H., & Hetzer, M. (2023). Caspase-mediated nuclear pore complex
trimming in cell differentiation and endoplasmic reticulum stress. ELife.
eLife Sciences Publications. https://doi.org/10.7554/eLife.89066
chicago: Cho, Ukrae H., and Martin Hetzer. “Caspase-Mediated Nuclear Pore Complex
Trimming in Cell Differentiation and Endoplasmic Reticulum Stress.” ELife.
eLife Sciences Publications, 2023. https://doi.org/10.7554/eLife.89066.
ieee: U. H. Cho and M. Hetzer, “Caspase-mediated nuclear pore complex trimming in
cell differentiation and endoplasmic reticulum stress,” eLife, vol. 12.
eLife Sciences Publications, 2023.
ista: Cho UH, Hetzer M. 2023. Caspase-mediated nuclear pore complex trimming in
cell differentiation and endoplasmic reticulum stress. eLife. 12, RP89066.
mla: Cho, Ukrae H., and Martin Hetzer. “Caspase-Mediated Nuclear Pore Complex Trimming
in Cell Differentiation and Endoplasmic Reticulum Stress.” ELife, vol.
12, RP89066, eLife Sciences Publications, 2023, doi:10.7554/eLife.89066.
short: U.H. Cho, M. Hetzer, ELife 12 (2023).
corr_author: '1'
date_created: 2023-09-10T22:01:11Z
date_published: 2023-09-04T00:00:00Z
date_updated: 2024-10-09T21:06:57Z
day: '04'
ddc:
- '570'
department:
- _id: MaHe
doi: 10.7554/eLife.89066
external_id:
pmid:
- '37665327'
file:
- access_level: open_access
checksum: db24bf3d595507387b48d3799c33e289
content_type: application/pdf
creator: dernst
date_created: 2023-09-15T06:59:10Z
date_updated: 2023-09-15T06:59:10Z
file_id: '14336'
file_name: 2023_eLife_Cho.pdf
file_size: 3703097
relation: main_file
success: 1
file_date_updated: 2023-09-15T06:59:10Z
has_accepted_license: '1'
intvolume: ' 12'
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
pmid: 1
publication: eLife
publication_identifier:
eissn:
- 2050-084X
publication_status: published
publisher: eLife Sciences Publications
quality_controlled: '1'
scopus_import: '1'
status: public
title: Caspase-mediated nuclear pore complex trimming in cell differentiation and
endoplasmic reticulum stress
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 12
year: '2023'
...
---
_id: '14868'
abstract:
- lang: eng
text: The role of nuclear pore complexes (NPCs) in genome organization remains poorly
characterized due to technical limitations in probing genome-wide protein-DNA
interactions specific to the nuclear periphery. Here, we developed a new sensitive
method, NPC-DamID, which combines in vitro reconstitution of nuclear import and
DamID technology. The fixation-free method identifies chromatin interactions at
the NPCs in intact nuclei from cells and tissues. We found that NPCs are preferentially
associated with common and hierarchically arranged super-enhancers (SEs) across
multiple cell types. We also uncovered phase-separated condensates at NPCs that
compartmentalize and concentrate transcriptional coactivators and structural proteins
at SE-regulated genes. Our results support NPCs as anchoring sites for SE regulatory
hubs and cell-type-specific transcriptional control.
acknowledgement: "This work was supported by M.H.’s NIH R01 grants (NS096786, GM126829)
and Salk Cancer Center Support Grant P30 CA014195. M.H. also received financial
support from the W.M. Keck Foundation and the NOMIS Foundation. Further, M.H. received
support from the AHA-Allen Initiative in Brain Health and Cognitive Impairment award
made jointly through the American Heart Association and The Paul G. Allen Frontiers
Group (19PABH134610000).\r\n\r\nS.T. and J.C. were supported by Salk’s Women & Science
Awards. S.T. also received financial support from the Hewitt Foundation fellowship,
and J.C. is a Paul F. Glenn Biology of Aging fellow. J.H. was supported by the National
Natural Science Foundation of China (31871317 and 32070635).\r\n\r\nWe thank Roberta
Schulte for assistance with in vitro transport assays, for comments that greatly
improved the manuscript, and for helping refine the figures presented in this work.
We thank Shefali Krishna for creating the diagram for the NPC-DamID method, for
her input on super-resolution microscopy analysis, and her insightful comments on
this manuscript. We thank all members of the Hetzer lab for helpful discussions
of these research ideas and their thoughtful comments on this manuscript. We are
also grateful to Salk’s core facilities for their assistance. Specifically, we thank
the Next Generation Sequencing Core (NGS) for sequencing our DamID and RNA NGS libraries,
the Advanced Biophotonics Core for assistance with super-resolution microscopy,
and the Razavi Newman Integrative Genomics and Bioinformatics Core (IGC) for their
input on analysis methods for DamID experiments."
article_processing_charge: Yes
article_type: original
author:
- first_name: Swati
full_name: Tyagi, Swati
last_name: Tyagi
- first_name: Juliana S.
full_name: Capitanio, Juliana S.
last_name: Capitanio
- first_name: Jiawei
full_name: Xu, Jiawei
last_name: Xu
- first_name: Fei
full_name: Chen, Fei
last_name: Chen
- first_name: Rahul
full_name: Sharma, Rahul
last_name: Sharma
- first_name: Jialiang
full_name: Huang, Jialiang
last_name: Huang
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Tyagi S, Capitanio JS, Xu J, et al. High-precision mapping of nuclear pore-chromatin
interactions reveals new principles of genome organization at the nuclear envelope.
eLife. 2023. doi:10.7554/elife.87462
apa: Tyagi, S., Capitanio, J. S., Xu, J., Chen, F., Sharma, R., Huang, J., &
Hetzer, M. (2023). High-precision mapping of nuclear pore-chromatin interactions
reveals new principles of genome organization at the nuclear envelope. ELife.
eLife Sciences Publications. https://doi.org/10.7554/elife.87462
chicago: Tyagi, Swati, Juliana S. Capitanio, Jiawei Xu, Fei Chen, Rahul Sharma,
Jialiang Huang, and Martin Hetzer. “High-Precision Mapping of Nuclear Pore-Chromatin
Interactions Reveals New Principles of Genome Organization at the Nuclear Envelope.”
ELife. eLife Sciences Publications, 2023. https://doi.org/10.7554/elife.87462.
ieee: S. Tyagi et al., “High-precision mapping of nuclear pore-chromatin
interactions reveals new principles of genome organization at the nuclear envelope,”
eLife. eLife Sciences Publications, 2023.
ista: Tyagi S, Capitanio JS, Xu J, Chen F, Sharma R, Huang J, Hetzer M. 2023. High-precision
mapping of nuclear pore-chromatin interactions reveals new principles of genome
organization at the nuclear envelope. eLife.
mla: Tyagi, Swati, et al. “High-Precision Mapping of Nuclear Pore-Chromatin Interactions
Reveals New Principles of Genome Organization at the Nuclear Envelope.” ELife,
eLife Sciences Publications, 2023, doi:10.7554/elife.87462.
short: S. Tyagi, J.S. Capitanio, J. Xu, F. Chen, R. Sharma, J. Huang, M. Hetzer,
ELife (2023).
corr_author: '1'
date_created: 2024-01-22T12:21:56Z
date_published: 2023-06-23T00:00:00Z
date_updated: 2024-07-31T11:56:25Z
day: '23'
department:
- _id: MaHe
doi: 10.7554/elife.87462
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.7554/eLife.87462.1
month: '06'
oa: 1
oa_version: Submitted Version
publication: eLife
publication_status: epub_ahead
publisher: eLife Sciences Publications
status: public
title: High-precision mapping of nuclear pore-chromatin interactions reveals new principles
of genome organization at the nuclear envelope
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2023'
...
---
_id: '11052'
abstract:
- lang: eng
text: In order to combat molecular damage, most cellular proteins undergo rapid
turnover. We have previously identified large nuclear protein assemblies that
can persist for years in post-mitotic tissues and are subject to age-related decline.
Here, we report that mitochondria can be long lived in the mouse brain and reveal
that specific mitochondrial proteins have half-lives longer than the average proteome.
These mitochondrial long-lived proteins (mitoLLPs) are core components of the
electron transport chain (ETC) and display increased longevity in respiratory
supercomplexes. We find that COX7C, a mitoLLP that forms a stable contact site
between complexes I and IV, is required for complex IV and supercomplex assembly.
Remarkably, even upon depletion of COX7C transcripts, ETC function is maintained
for days, effectively uncoupling mitochondrial function from ongoing transcription
of its mitoLLPs. Our results suggest that modulating protein longevity within
the ETC is critical for mitochondrial proteome maintenance and the robustness
of mitochondrial function.
article_processing_charge: No
article_type: original
author:
- first_name: Shefali
full_name: Krishna, Shefali
last_name: Krishna
- first_name: Rafael
full_name: Arrojo e Drigo, Rafael
last_name: Arrojo e Drigo
- first_name: Juliana S.
full_name: Capitanio, Juliana S.
last_name: Capitanio
- first_name: Ranjan
full_name: Ramachandra, Ranjan
last_name: Ramachandra
- first_name: Mark
full_name: Ellisman, Mark
last_name: Ellisman
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Krishna S, Arrojo e Drigo R, Capitanio JS, Ramachandra R, Ellisman M, Hetzer
M. Identification of long-lived proteins in the mitochondria reveals increased
stability of the electron transport chain. Developmental Cell. 2021;56(21):P2952-2965.e9.
doi:10.1016/j.devcel.2021.10.008
apa: Krishna, S., Arrojo e Drigo, R., Capitanio, J. S., Ramachandra, R., Ellisman,
M., & Hetzer, M. (2021). Identification of long-lived proteins in the mitochondria
reveals increased stability of the electron transport chain. Developmental
Cell. Elsevier. https://doi.org/10.1016/j.devcel.2021.10.008
chicago: Krishna, Shefali, Rafael Arrojo e Drigo, Juliana S. Capitanio, Ranjan Ramachandra,
Mark Ellisman, and Martin Hetzer. “Identification of Long-Lived Proteins in the
Mitochondria Reveals Increased Stability of the Electron Transport Chain.” Developmental
Cell. Elsevier, 2021. https://doi.org/10.1016/j.devcel.2021.10.008.
ieee: S. Krishna, R. Arrojo e Drigo, J. S. Capitanio, R. Ramachandra, M. Ellisman,
and M. Hetzer, “Identification of long-lived proteins in the mitochondria reveals
increased stability of the electron transport chain,” Developmental Cell,
vol. 56, no. 21. Elsevier, p. P2952–2965.e9, 2021.
ista: Krishna S, Arrojo e Drigo R, Capitanio JS, Ramachandra R, Ellisman M, Hetzer
M. 2021. Identification of long-lived proteins in the mitochondria reveals increased
stability of the electron transport chain. Developmental Cell. 56(21), P2952–2965.e9.
mla: Krishna, Shefali, et al. “Identification of Long-Lived Proteins in the Mitochondria
Reveals Increased Stability of the Electron Transport Chain.” Developmental
Cell, vol. 56, no. 21, Elsevier, 2021, p. P2952–2965.e9, doi:10.1016/j.devcel.2021.10.008.
short: S. Krishna, R. Arrojo e Drigo, J.S. Capitanio, R. Ramachandra, M. Ellisman,
M. Hetzer, Developmental Cell 56 (2021) P2952–2965.e9.
date_created: 2022-04-07T07:43:14Z
date_published: 2021-11-08T00:00:00Z
date_updated: 2025-12-15T10:01:56Z
day: '08'
department:
- _id: MaHe
doi: 10.1016/j.devcel.2021.10.008
extern: '1'
external_id:
pmid:
- '34715012'
intvolume: ' 56'
issue: '21'
keyword:
- Developmental Biology
- Cell Biology
- General Biochemistry
- Genetics and Molecular Biology
- Molecular Biology
language:
- iso: eng
month: '11'
oa_version: None
page: P2952-2965.e9
pmid: 1
publication: Developmental Cell
publication_identifier:
issn:
- 1534-5807
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Identification of long-lived proteins in the mitochondria reveals increased
stability of the electron transport chain
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 56
year: '2021'
...
---
_id: '11062'
abstract:
- lang: eng
text: Most neurons are not replaced during an animal’s lifetime. This nondividing
state is characterized by extreme longevity and age-dependent decline of key regulatory
proteins. To study the lifespans of cells and proteins in adult tissues, we combined
isotope labeling of mice with a hybrid imaging method (MIMS-EM). Using 15N mapping,
we show that liver and pancreas are composed of cells with vastly different ages,
many as old as the animal. Strikingly, we also found that a subset of fibroblasts
and endothelial cells, both known for their replicative potential, are characterized
by the absence of cell division during adulthood. In addition, we show that the
primary cilia of beta cells and neurons contains different structural regions
with vastly different lifespans. Based on these results, we propose that age mosaicism
across multiple scales is a fundamental principle of adult tissue, cell, and protein
complex organization.
article_processing_charge: No
article_type: original
author:
- first_name: Rafael
full_name: Arrojo e Drigo, Rafael
last_name: Arrojo e Drigo
- first_name: Varda
full_name: Lev-Ram, Varda
last_name: Lev-Ram
- first_name: Swati
full_name: Tyagi, Swati
last_name: Tyagi
- first_name: Ranjan
full_name: Ramachandra, Ranjan
last_name: Ramachandra
- first_name: Thomas
full_name: Deerinck, Thomas
last_name: Deerinck
- first_name: Eric
full_name: Bushong, Eric
last_name: Bushong
- first_name: Sebastien
full_name: Phan, Sebastien
last_name: Phan
- first_name: Victoria
full_name: Orphan, Victoria
last_name: Orphan
- first_name: Claude
full_name: Lechene, Claude
last_name: Lechene
- first_name: Mark H.
full_name: Ellisman, Mark H.
last_name: Ellisman
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Arrojo e Drigo R, Lev-Ram V, Tyagi S, et al. Age mosaicism across multiple
scales in adult tissues. Cell Metabolism. 2019;30(2):343-351.e3. doi:10.1016/j.cmet.2019.05.010
apa: Arrojo e Drigo, R., Lev-Ram, V., Tyagi, S., Ramachandra, R., Deerinck, T.,
Bushong, E., … Hetzer, M. (2019). Age mosaicism across multiple scales in adult
tissues. Cell Metabolism. Elsevier. https://doi.org/10.1016/j.cmet.2019.05.010
chicago: Arrojo e Drigo, Rafael, Varda Lev-Ram, Swati Tyagi, Ranjan Ramachandra,
Thomas Deerinck, Eric Bushong, Sebastien Phan, et al. “Age Mosaicism across Multiple
Scales in Adult Tissues.” Cell Metabolism. Elsevier, 2019. https://doi.org/10.1016/j.cmet.2019.05.010.
ieee: R. Arrojo e Drigo et al., “Age mosaicism across multiple scales in
adult tissues,” Cell Metabolism, vol. 30, no. 2. Elsevier, p. 343–351.e3,
2019.
ista: Arrojo e Drigo R, Lev-Ram V, Tyagi S, Ramachandra R, Deerinck T, Bushong E,
Phan S, Orphan V, Lechene C, Ellisman MH, Hetzer M. 2019. Age mosaicism across
multiple scales in adult tissues. Cell Metabolism. 30(2), 343–351.e3.
mla: Arrojo e Drigo, Rafael, et al. “Age Mosaicism across Multiple Scales in Adult
Tissues.” Cell Metabolism, vol. 30, no. 2, Elsevier, 2019, p. 343–351.e3,
doi:10.1016/j.cmet.2019.05.010.
short: R. Arrojo e Drigo, V. Lev-Ram, S. Tyagi, R. Ramachandra, T. Deerinck, E.
Bushong, S. Phan, V. Orphan, C. Lechene, M.H. Ellisman, M. Hetzer, Cell Metabolism
30 (2019) 343–351.e3.
date_created: 2022-04-07T07:45:21Z
date_published: 2019-08-06T00:00:00Z
date_updated: 2025-12-15T10:02:11Z
day: '06'
department:
- _id: MaHe
doi: 10.1016/j.cmet.2019.05.010
extern: '1'
external_id:
pmid:
- '31178361'
intvolume: ' 30'
issue: '2'
keyword:
- Cell Biology
- Molecular Biology
- Physiology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.cmet.2019.05.010
month: '08'
oa: 1
oa_version: Published Version
page: 343-351.e3
pmid: 1
publication: Cell Metabolism
publication_identifier:
issn:
- 1550-4131
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Age mosaicism across multiple scales in adult tissues
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 30
year: '2019'
...
---
_id: '11087'
abstract:
- lang: eng
text: Intracellular proteins with long lifespans have recently been linked to age-dependent
defects, ranging from decreased fertility to the functional decline of neurons.
Why long-lived proteins exist in metabolically active cellular environments and
how they are maintained over time remains poorly understood. Here, we provide
a system-wide identification of proteins with exceptional lifespans in the rat
brain. These proteins are inefficiently replenished despite being translated robustly
throughout adulthood. Using nucleoporins as a paradigm for long-term protein persistence,
we found that nuclear pore complexes (NPCs) are maintained over a cell’s life
through slow but finite exchange of even its most stable subcomplexes. This maintenance
is limited, however, as some nucleoporin levels decrease during aging, providing
a rationale for the previously observed age-dependent deterioration of NPC function.
Our identification of a long-lived proteome reveals cellular components that are
at increased risk for damage accumulation, linking long-term protein persistence
to the cellular aging process.
article_processing_charge: No
article_type: original
author:
- first_name: Brandon H.
full_name: Toyama, Brandon H.
last_name: Toyama
- first_name: Jeffrey N.
full_name: Savas, Jeffrey N.
last_name: Savas
- first_name: Sung Kyu
full_name: Park, Sung Kyu
last_name: Park
- first_name: Michael S.
full_name: Harris, Michael S.
last_name: Harris
- first_name: Nicholas T.
full_name: Ingolia, Nicholas T.
last_name: Ingolia
- first_name: John R.
full_name: Yates, John R.
last_name: Yates
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Toyama BH, Savas JN, Park SK, et al. Identification of long-lived proteins
reveals exceptional stability of essential cellular structures. Cell. 2013;154(5):971-982.
doi:10.1016/j.cell.2013.07.037
apa: Toyama, B. H., Savas, J. N., Park, S. K., Harris, M. S., Ingolia, N. T., Yates,
J. R., & Hetzer, M. (2013). Identification of long-lived proteins reveals
exceptional stability of essential cellular structures. Cell. Elsevier.
https://doi.org/10.1016/j.cell.2013.07.037
chicago: Toyama, Brandon H., Jeffrey N. Savas, Sung Kyu Park, Michael S. Harris,
Nicholas T. Ingolia, John R. Yates, and Martin Hetzer. “Identification of Long-Lived
Proteins Reveals Exceptional Stability of Essential Cellular Structures.” Cell.
Elsevier, 2013. https://doi.org/10.1016/j.cell.2013.07.037.
ieee: B. H. Toyama et al., “Identification of long-lived proteins reveals
exceptional stability of essential cellular structures,” Cell, vol. 154,
no. 5. Elsevier, pp. 971–982, 2013.
ista: Toyama BH, Savas JN, Park SK, Harris MS, Ingolia NT, Yates JR, Hetzer M. 2013.
Identification of long-lived proteins reveals exceptional stability of essential
cellular structures. Cell. 154(5), 971–982.
mla: Toyama, Brandon H., et al. “Identification of Long-Lived Proteins Reveals Exceptional
Stability of Essential Cellular Structures.” Cell, vol. 154, no. 5, Elsevier,
2013, pp. 971–82, doi:10.1016/j.cell.2013.07.037.
short: B.H. Toyama, J.N. Savas, S.K. Park, M.S. Harris, N.T. Ingolia, J.R. Yates,
M. Hetzer, Cell 154 (2013) 971–982.
date_created: 2022-04-07T07:51:08Z
date_published: 2013-08-29T00:00:00Z
date_updated: 2025-12-15T10:02:46Z
day: '29'
department:
- _id: MaHe
doi: 10.1016/j.cell.2013.07.037
extern: '1'
external_id:
pmid:
- '23993091'
intvolume: ' 154'
issue: '5'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.cell.2013.07.037
month: '08'
oa: 1
oa_version: Published Version
page: 971-982
pmid: 1
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Identification of long-lived proteins reveals exceptional stability of essential
cellular structures
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 154
year: '2013'
...
---
_id: '11092'
abstract:
- lang: eng
text: To combat the functional decline of the proteome, cells use the process of
protein turnover to replace potentially impaired polypeptides with new functional
copies. We found that extremely long-lived proteins (ELLPs) did not turn over
in postmitotic cells of the rat central nervous system. These ELLPs were associated
with chromatin and the nuclear pore complex, the central transport channels that
mediate all molecular trafficking in and out of the nucleus. The longevity of
these proteins would be expected to expose them to potentially harmful metabolites,
putting them at risk of accumulating damage over extended periods of time. Thus,
it is possible that failure to maintain proper levels and functional integrity
of ELLPs in nonproliferative cells might contribute to age-related deterioration
in cell and tissue function.
article_processing_charge: No
article_type: letter_note
author:
- first_name: Jeffrey N.
full_name: Savas, Jeffrey N.
last_name: Savas
- first_name: Brandon H.
full_name: Toyama, Brandon H.
last_name: Toyama
- first_name: Tao
full_name: Xu, Tao
last_name: Xu
- first_name: John R.
full_name: Yates, John R.
last_name: Yates
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Savas JN, Toyama BH, Xu T, Yates JR, Hetzer M. Extremely long-lived nuclear
pore proteins in the rat brain. Science. 2012;335(6071):942-942. doi:10.1126/science.1217421
apa: Savas, J. N., Toyama, B. H., Xu, T., Yates, J. R., & Hetzer, M. (2012).
Extremely long-lived nuclear pore proteins in the rat brain. Science. American
Association for the Advancement of Science. https://doi.org/10.1126/science.1217421
chicago: Savas, Jeffrey N., Brandon H. Toyama, Tao Xu, John R. Yates, and Martin
Hetzer. “Extremely Long-Lived Nuclear Pore Proteins in the Rat Brain.” Science.
American Association for the Advancement of Science, 2012. https://doi.org/10.1126/science.1217421.
ieee: J. N. Savas, B. H. Toyama, T. Xu, J. R. Yates, and M. Hetzer, “Extremely long-lived
nuclear pore proteins in the rat brain,” Science, vol. 335, no. 6071. American
Association for the Advancement of Science, pp. 942–942, 2012.
ista: Savas JN, Toyama BH, Xu T, Yates JR, Hetzer M. 2012. Extremely long-lived
nuclear pore proteins in the rat brain. Science. 335(6071), 942–942.
mla: Savas, Jeffrey N., et al. “Extremely Long-Lived Nuclear Pore Proteins in the
Rat Brain.” Science, vol. 335, no. 6071, American Association for the Advancement
of Science, 2012, pp. 942–942, doi:10.1126/science.1217421.
short: J.N. Savas, B.H. Toyama, T. Xu, J.R. Yates, M. Hetzer, Science 335 (2012)
942–942.
date_created: 2022-04-07T07:52:01Z
date_published: 2012-02-02T00:00:00Z
date_updated: 2025-12-15T10:03:06Z
day: '02'
department:
- _id: MaHe
doi: 10.1126/science.1217421
extern: '1'
external_id:
pmid:
- '22300851'
intvolume: ' 335'
issue: '6071'
language:
- iso: eng
month: '02'
oa_version: None
page: 942-942
pmid: 1
publication: Science
publication_identifier:
eissn:
- 1095-9203
issn:
- 0036-8075
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
scopus_import: '1'
status: public
title: Extremely long-lived nuclear pore proteins in the rat brain
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 335
year: '2012'
...