---
_id: '15141'
abstract:
- lang: eng
  text: We reveal the cryo-electron microscopy structure of a type IV-B CRISPR ribonucleoprotein
    (RNP) complex (Csf) at 3.9-Å resolution. The complex best resembles the type III-A
    CRISPR Csm effector complex, consisting of a Cas7-like (Csf2) filament intertwined
    with a small subunit (Cas11) filament, but the complex lacks subunits for RNA
    processing and target DNA cleavage. Surprisingly, instead of assembling around
    a CRISPR-derived RNA (crRNA), the complex assembles upon heterogeneous RNA of
    a regular length arranged in a pseudo-A-form configuration. These findings provide
    a high-resolution glimpse into the assembly and function of enigmatic type IV
    CRISPR systems, expanding our understanding of class I CRISPR-Cas system architecture,
    and suggesting a function for type IV-B RNPs that may be distinct from other class
    1 CRISPR-associated systems.
article_number: '102201'
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Yi
  full_name: Zhou, Yi
  last_name: Zhou
- first_name: Jack Peter Kelly
  full_name: Bravo, Jack Peter Kelly
  id: 96aecfa5-8931-11ee-af30-aa6a5d6eee0e
  last_name: Bravo
  orcid: 0000-0003-0456-0753
- first_name: Hannah N.
  full_name: Taylor, Hannah N.
  last_name: Taylor
- first_name: Jurre A.
  full_name: Steens, Jurre A.
  last_name: Steens
- first_name: Ryan N.
  full_name: Jackson, Ryan N.
  last_name: Jackson
- first_name: Raymond H.J.
  full_name: Staals, Raymond H.J.
  last_name: Staals
- first_name: David W.
  full_name: Taylor, David W.
  last_name: Taylor
citation:
  ama: Zhou Y, Bravo JPK, Taylor HN, et al. Structure of a type IV CRISPR-Cas ribonucleoprotein
    complex. <i>iScience</i>. 2021;24(3). doi:<a href="https://doi.org/10.1016/j.isci.2021.102201">10.1016/j.isci.2021.102201</a>
  apa: Zhou, Y., Bravo, J. P. K., Taylor, H. N., Steens, J. A., Jackson, R. N., Staals,
    R. H. J., &#38; Taylor, D. W. (2021). Structure of a type IV CRISPR-Cas ribonucleoprotein
    complex. <i>IScience</i>. Elsevier. <a href="https://doi.org/10.1016/j.isci.2021.102201">https://doi.org/10.1016/j.isci.2021.102201</a>
  chicago: Zhou, Yi, Jack Peter Kelly Bravo, Hannah N. Taylor, Jurre A. Steens, Ryan
    N. Jackson, Raymond H.J. Staals, and David W. Taylor. “Structure of a Type IV
    CRISPR-Cas Ribonucleoprotein Complex.” <i>IScience</i>. Elsevier, 2021. <a href="https://doi.org/10.1016/j.isci.2021.102201">https://doi.org/10.1016/j.isci.2021.102201</a>.
  ieee: Y. Zhou <i>et al.</i>, “Structure of a type IV CRISPR-Cas ribonucleoprotein
    complex,” <i>iScience</i>, vol. 24, no. 3. Elsevier, 2021.
  ista: Zhou Y, Bravo JPK, Taylor HN, Steens JA, Jackson RN, Staals RHJ, Taylor DW.
    2021. Structure of a type IV CRISPR-Cas ribonucleoprotein complex. iScience. 24(3),
    102201.
  mla: Zhou, Yi, et al. “Structure of a Type IV CRISPR-Cas Ribonucleoprotein Complex.”
    <i>IScience</i>, vol. 24, no. 3, 102201, Elsevier, 2021, doi:<a href="https://doi.org/10.1016/j.isci.2021.102201">10.1016/j.isci.2021.102201</a>.
  short: Y. Zhou, J.P.K. Bravo, H.N. Taylor, J.A. Steens, R.N. Jackson, R.H.J. Staals,
    D.W. Taylor, IScience 24 (2021).
date_created: 2024-03-20T10:43:00Z
date_published: 2021-03-19T00:00:00Z
date_updated: 2024-06-04T05:56:45Z
day: '19'
doi: 10.1016/j.isci.2021.102201
extern: '1'
external_id:
  pmid:
  - '33733066'
intvolume: '        24'
issue: '3'
keyword:
- Multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1016/j.isci.2021.102201
month: '03'
oa: 1
oa_version: Published Version
pmid: 1
publication: iScience
publication_identifier:
  issn:
  - 2589-0042
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Structure of a type IV CRISPR-Cas ribonucleoprotein complex
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 24
year: '2021'
...
---
_id: '6451'
abstract:
- lang: eng
  text: Epidermal growth factor receptor (EGFR) signaling controls skin development
    and homeostasis inmice and humans, and its deficiency causes severe skin inflammation,
    which might affect epidermalstem cell behavior. Here, we describe the inflammation-independent
    effects of EGFR deficiency dur-ing skin morphogenesis and in adult hair follicle
    stem cells. Expression and alternative splicing analysisof RNA sequencing data
    from interfollicular epidermis and outer root sheath indicate that EGFR con-trols
    genes involved in epidermal differentiation and also in centrosome function, DNA
    damage, cellcycle, and apoptosis. Genetic experiments employingp53deletion in
    EGFR-deficient epidermis revealthat EGFR signaling exhibitsp53-dependent functions
    in proliferative epidermal compartments, aswell asp53-independent functions in
    differentiated hair shaft keratinocytes. Loss of EGFR leads toabsence of LEF1
    protein specifically in the innermost epithelial hair layers, resulting in disorganizationof
    medulla cells. Thus, our results uncover important spatial and temporal features
    of cell-autonomousEGFR functions in the epidermis.
article_processing_charge: No
author:
- first_name: Nicole
  full_name: Amberg, Nicole
  id: 4CD6AAC6-F248-11E8-B48F-1D18A9856A87
  last_name: Amberg
  orcid: 0000-0002-3183-8207
- first_name: Panagiota A.
  full_name: Sotiropoulou, Panagiota A.
  last_name: Sotiropoulou
- first_name: Gerwin
  full_name: Heller, Gerwin
  last_name: Heller
- first_name: Beate M.
  full_name: Lichtenberger, Beate M.
  last_name: Lichtenberger
- first_name: Martin
  full_name: Holcmann, Martin
  last_name: Holcmann
- first_name: Bahar
  full_name: Camurdanoglu, Bahar
  last_name: Camurdanoglu
- first_name: Temenuschka
  full_name: Baykuscheva-Gentscheva, Temenuschka
  last_name: Baykuscheva-Gentscheva
- first_name: Cedric
  full_name: Blanpain, Cedric
  last_name: Blanpain
- first_name: Maria
  full_name: Sibilia, Maria
  last_name: Sibilia
citation:
  ama: Amberg N, Sotiropoulou PA, Heller G, et al. EGFR controls hair shaft differentiation
    in a p53-independent manner. <i>iScience</i>. 2019;15:243-256. doi:<a href="https://doi.org/10.1016/j.isci.2019.04.018">10.1016/j.isci.2019.04.018</a>
  apa: Amberg, N., Sotiropoulou, P. A., Heller, G., Lichtenberger, B. M., Holcmann,
    M., Camurdanoglu, B., … Sibilia, M. (2019). EGFR controls hair shaft differentiation
    in a p53-independent manner. <i>IScience</i>. Elsevier. <a href="https://doi.org/10.1016/j.isci.2019.04.018">https://doi.org/10.1016/j.isci.2019.04.018</a>
  chicago: Amberg, Nicole, Panagiota A. Sotiropoulou, Gerwin Heller, Beate M. Lichtenberger,
    Martin Holcmann, Bahar Camurdanoglu, Temenuschka Baykuscheva-Gentscheva, Cedric
    Blanpain, and Maria Sibilia. “EGFR Controls Hair Shaft Differentiation in a P53-Independent
    Manner.” <i>IScience</i>. Elsevier, 2019. <a href="https://doi.org/10.1016/j.isci.2019.04.018">https://doi.org/10.1016/j.isci.2019.04.018</a>.
  ieee: N. Amberg <i>et al.</i>, “EGFR controls hair shaft differentiation in a p53-independent
    manner,” <i>iScience</i>, vol. 15. Elsevier, pp. 243–256, 2019.
  ista: Amberg N, Sotiropoulou PA, Heller G, Lichtenberger BM, Holcmann M, Camurdanoglu
    B, Baykuscheva-Gentscheva T, Blanpain C, Sibilia M. 2019. EGFR controls hair shaft
    differentiation in a p53-independent manner. iScience. 15, 243–256.
  mla: Amberg, Nicole, et al. “EGFR Controls Hair Shaft Differentiation in a P53-Independent
    Manner.” <i>IScience</i>, vol. 15, Elsevier, 2019, pp. 243–56, doi:<a href="https://doi.org/10.1016/j.isci.2019.04.018">10.1016/j.isci.2019.04.018</a>.
  short: N. Amberg, P.A. Sotiropoulou, G. Heller, B.M. Lichtenberger, M. Holcmann,
    B. Camurdanoglu, T. Baykuscheva-Gentscheva, C. Blanpain, M. Sibilia, IScience
    15 (2019) 243–256.
date_created: 2019-05-14T11:47:40Z
date_published: 2019-05-31T00:00:00Z
date_updated: 2023-09-08T11:38:04Z
day: '31'
ddc:
- '570'
department:
- _id: SiHi
doi: 10.1016/j.isci.2019.04.018
external_id:
  isi:
  - '000470104600022'
file:
- access_level: open_access
  checksum: a9ad2296726c9474ad5860c9c2f53622
  content_type: application/pdf
  creator: dernst
  date_created: 2019-05-14T11:51:51Z
  date_updated: 2020-07-14T12:47:30Z
  file_id: '6452'
  file_name: 2019_iScience_Amberg.pdf
  file_size: 8365970
  relation: main_file
file_date_updated: 2020-07-14T12:47:30Z
has_accepted_license: '1'
intvolume: '        15'
isi: 1
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc-nd/4.0/
month: '05'
oa: 1
oa_version: Published Version
page: 243-256
publication: iScience
publication_identifier:
  issn:
  - 2589-0042
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: EGFR controls hair shaft differentiation in a p53-independent manner
tmp:
  image: /images/cc_by_nc_nd.png
  legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode
  name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
    (CC BY-NC-ND 4.0)
  short: CC BY-NC-ND (4.0)
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 15
year: '2019'
...
---
_id: '7391'
abstract:
- lang: eng
  text: Electron microscopy (EM) is a technology that enables visualization of single
    proteins at a nanometer resolution. However, current protein analysis by EM mainly
    relies on immunolabeling with gold-particle-conjugated antibodies, which is compromised
    by large size of antibody, precluding precise detection of protein location in
    biological samples. Here, we develop a specific chemical labeling method for EM
    detection of proteins at single-molecular level. Rational design of α-helical
    peptide tag and probe structure provided a complementary reaction pair that enabled
    specific cysteine conjugation of the tag. The developed chemical labeling with
    gold-nanoparticle-conjugated probe showed significantly higher labeling efficiency
    and detectability of high-density clusters of tag-fused G protein-coupled receptors
    in freeze-fracture replicas compared with immunogold labeling. Furthermore, in
    ultrathin sections, the spatial resolution of the chemical labeling was significantly
    higher than that of antibody-mediated labeling. These results demonstrate substantial
    advantages of the chemical labeling approach for single protein visualization
    by EM.
article_processing_charge: No
article_type: original
author:
- first_name: Shigekazu
  full_name: Tabata, Shigekazu
  id: 4427179E-F248-11E8-B48F-1D18A9856A87
  last_name: Tabata
- first_name: Marijo
  full_name: Jevtic, Marijo
  id: 4BE3BC94-F248-11E8-B48F-1D18A9856A87
  last_name: Jevtic
- first_name: Nobutaka
  full_name: Kurashige, Nobutaka
  last_name: Kurashige
- first_name: Hirokazu
  full_name: Fuchida, Hirokazu
  last_name: Fuchida
- first_name: Munetsugu
  full_name: Kido, Munetsugu
  last_name: Kido
- first_name: Kazushi
  full_name: Tani, Kazushi
  last_name: Tani
- first_name: Naoki
  full_name: Zenmyo, Naoki
  last_name: Zenmyo
- first_name: Shohei
  full_name: Uchinomiya, Shohei
  last_name: Uchinomiya
- first_name: Harumi
  full_name: Harada, Harumi
  id: 2E55CDF2-F248-11E8-B48F-1D18A9856A87
  last_name: Harada
  orcid: 0000-0001-7429-7896
- first_name: Makoto
  full_name: Itakura, Makoto
  last_name: Itakura
- first_name: Itaru
  full_name: Hamachi, Itaru
  last_name: Hamachi
- first_name: Ryuichi
  full_name: Shigemoto, Ryuichi
  id: 499F3ABC-F248-11E8-B48F-1D18A9856A87
  last_name: Shigemoto
  orcid: 0000-0001-8761-9444
- first_name: Akio
  full_name: Ojida, Akio
  last_name: Ojida
citation:
  ama: Tabata S, Jevtic M, Kurashige N, et al. Electron microscopic detection of single
    membrane proteins by a specific chemical labeling. <i>iScience</i>. 2019;22(12):256-268.
    doi:<a href="https://doi.org/10.1016/j.isci.2019.11.025">10.1016/j.isci.2019.11.025</a>
  apa: Tabata, S., Jevtic, M., Kurashige, N., Fuchida, H., Kido, M., Tani, K., … Ojida,
    A. (2019). Electron microscopic detection of single membrane proteins by a specific
    chemical labeling. <i>IScience</i>. Elsevier. <a href="https://doi.org/10.1016/j.isci.2019.11.025">https://doi.org/10.1016/j.isci.2019.11.025</a>
  chicago: Tabata, Shigekazu, Marijo Jevtic, Nobutaka Kurashige, Hirokazu Fuchida,
    Munetsugu Kido, Kazushi Tani, Naoki Zenmyo, et al. “Electron Microscopic Detection
    of Single Membrane Proteins by a Specific Chemical Labeling.” <i>IScience</i>.
    Elsevier, 2019. <a href="https://doi.org/10.1016/j.isci.2019.11.025">https://doi.org/10.1016/j.isci.2019.11.025</a>.
  ieee: S. Tabata <i>et al.</i>, “Electron microscopic detection of single membrane
    proteins by a specific chemical labeling,” <i>iScience</i>, vol. 22, no. 12. Elsevier,
    pp. 256–268, 2019.
  ista: Tabata S, Jevtic M, Kurashige N, Fuchida H, Kido M, Tani K, Zenmyo N, Uchinomiya
    S, Harada H, Itakura M, Hamachi I, Shigemoto R, Ojida A. 2019. Electron microscopic
    detection of single membrane proteins by a specific chemical labeling. iScience.
    22(12), 256–268.
  mla: Tabata, Shigekazu, et al. “Electron Microscopic Detection of Single Membrane
    Proteins by a Specific Chemical Labeling.” <i>IScience</i>, vol. 22, no. 12, Elsevier,
    2019, pp. 256–68, doi:<a href="https://doi.org/10.1016/j.isci.2019.11.025">10.1016/j.isci.2019.11.025</a>.
  short: S. Tabata, M. Jevtic, N. Kurashige, H. Fuchida, M. Kido, K. Tani, N. Zenmyo,
    S. Uchinomiya, H. Harada, M. Itakura, I. Hamachi, R. Shigemoto, A. Ojida, IScience
    22 (2019) 256–268.
corr_author: '1'
date_created: 2020-01-29T15:56:56Z
date_published: 2019-12-20T00:00:00Z
date_updated: 2026-04-27T22:30:31Z
day: '20'
ddc:
- '570'
department:
- _id: RySh
doi: 10.1016/j.isci.2019.11.025
ec_funded: 1
external_id:
  isi:
  - '000504652000020'
  pmid:
  - '31786521'
file:
- access_level: open_access
  checksum: f3e90056a49f09b205b1c4f8c739ffd1
  content_type: application/pdf
  creator: dernst
  date_created: 2020-02-04T10:48:36Z
  date_updated: 2020-07-14T12:47:57Z
  file_id: '7448'
  file_name: 2019_iScience_Tabata.pdf
  file_size: 7197776
  relation: main_file
file_date_updated: 2020-07-14T12:47:57Z
has_accepted_license: '1'
intvolume: '        22'
isi: 1
issue: '12'
language:
- iso: eng
license: https://creativecommons.org/licenses/by/4.0/
month: '12'
oa: 1
oa_version: Published Version
page: 256-268
pmid: 1
project:
- _id: 25CA28EA-B435-11E9-9278-68D0E5697425
  call_identifier: H2020
  grant_number: '694539'
  name: 'In situ analysis of single channel subunit composition in neurons: physiological
    implication in synaptic plasticity and behaviour'
- _id: 25CBA828-B435-11E9-9278-68D0E5697425
  call_identifier: H2020
  grant_number: '720270'
  name: Human Brain Project Specific Grant Agreement 1
publication: iScience
publication_identifier:
  issn:
  - 2589-0042
publication_status: published
publisher: Elsevier
quality_controlled: '1'
related_material:
  record:
  - id: '11393'
    relation: dissertation_contains
    status: public
scopus_import: '1'
status: public
title: Electron microscopic detection of single membrane proteins by a specific chemical
  labeling
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: 22
year: '2019'
...