---
_id: '9495'
abstract:
- lang: eng
text: RNA interference is a conserved process in which double-stranded RNA is processed
into 21–25 nucleotide siRNAs that trigger posttranscriptional gene silencing.
In addition, plants display a phenomenon termed RNA-directed DNA methylation (RdDM)
in which DNA with sequence identity to silenced RNA is de novo methylated at its
cytosine residues. This methylation is not only at canonical CpG sites but also
at cytosines in CpNpG and asymmetric sequence contexts. In this report, we study
the role of the DRM and CMT3 DNA methyltransferase genes in the initiation and
maintenance of RdDM. Neither drm nor cmt3 mutants affected the maintenance of
preestablished RNA-directed CpG methylation. However, drm mutants showed a nearly
complete loss of asymmetric methylation and a partial loss of CpNpG methylation.
The remaining asymmetric and CpNpG methylation was dependent on the activity of
CMT3, showing that DRM and CMT3 act redundantly to maintain non-CpG methylation.
These DNA methyltransferases appear to act downstream of siRNAs, since drm1 drm2
cmt3 triple mutants show a lack of non-CpG methylation but elevated levels of
siRNAs. Finally, we demonstrate that DRM activity is required for the initial
establishment of RdDM in all sequence contexts including CpG, CpNpG, and asymmetric
sites.
article_processing_charge: No
article_type: original
author:
- first_name: Xiaofeng
full_name: Cao, Xiaofeng
last_name: Cao
- first_name: Werner
full_name: Aufsatz, Werner
last_name: Aufsatz
- first_name: Daniel
full_name: Zilberman, Daniel
id: 6973db13-dd5f-11ea-814e-b3e5455e9ed1
last_name: Zilberman
orcid: 0000-0002-0123-8649
- first_name: M.Florian
full_name: Mette, M.Florian
last_name: Mette
- first_name: Michael S.
full_name: Huang, Michael S.
last_name: Huang
- first_name: Marjori
full_name: Matzke, Marjori
last_name: Matzke
- first_name: Steven E.
full_name: Jacobsen, Steven E.
last_name: Jacobsen
citation:
ama: Cao X, Aufsatz W, Zilberman D, et al. Role of the DRM and CMT3 methyltransferases
in RNA-directed DNA methylation. Current Biology. 2003;13(24):2212-2217.
doi:10.1016/j.cub.2003.11.052
apa: Cao, X., Aufsatz, W., Zilberman, D., Mette, M. F., Huang, M. S., Matzke, M.,
& Jacobsen, S. E. (2003). Role of the DRM and CMT3 methyltransferases in RNA-directed
DNA methylation. Current Biology. Elsevier. https://doi.org/10.1016/j.cub.2003.11.052
chicago: Cao, Xiaofeng, Werner Aufsatz, Daniel Zilberman, M.Florian Mette, Michael
S. Huang, Marjori Matzke, and Steven E. Jacobsen. “Role of the DRM and CMT3 Methyltransferases
in RNA-Directed DNA Methylation.” Current Biology. Elsevier, 2003. https://doi.org/10.1016/j.cub.2003.11.052.
ieee: X. Cao et al., “Role of the DRM and CMT3 methyltransferases in RNA-directed
DNA methylation,” Current Biology, vol. 13, no. 24. Elsevier, pp. 2212–2217,
2003.
ista: Cao X, Aufsatz W, Zilberman D, Mette MF, Huang MS, Matzke M, Jacobsen SE.
2003. Role of the DRM and CMT3 methyltransferases in RNA-directed DNA methylation.
Current Biology. 13(24), 2212–2217.
mla: Cao, Xiaofeng, et al. “Role of the DRM and CMT3 Methyltransferases in RNA-Directed
DNA Methylation.” Current Biology, vol. 13, no. 24, Elsevier, 2003, pp.
2212–17, doi:10.1016/j.cub.2003.11.052.
short: X. Cao, W. Aufsatz, D. Zilberman, M.F. Mette, M.S. Huang, M. Matzke, S.E.
Jacobsen, Current Biology 13 (2003) 2212–2217.
date_created: 2021-06-07T10:43:02Z
date_published: 2003-12-16T00:00:00Z
date_updated: 2021-12-14T08:41:38Z
day: '16'
department:
- _id: DaZi
doi: 10.1016/j.cub.2003.11.052
extern: '1'
external_id:
pmid:
- '14680640'
fulldoi: https://doi.org/10.1016/j.cub.2003.11.052
intvolume: ' 13'
issue: '24'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.cub.2003.11.052
month: '12'
oa: 1
oa_version: Published Version
page: 2212-2217
pmid: 1
publication: Current Biology
publication_identifier:
eissn:
- 1879-0445
issn:
- 0960-9822
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Role of the DRM and CMT3 methyltransferases in RNA-directed DNA methylation
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 13
year: '2003'
...
---
_id: '4169'
abstract:
- lang: eng
text: 'Background: During vertebrate gastrulation, cell polarization and migration
are core components in the cellular rearrangements that lead to the formation
of the three germ layers, ectoderm, mesoderm, and endoderm. Previous studies have
implicated the Wnt/planar cell polarity (PCP) signaling pathway in controlling
cell morphology and movement during gastrulation. However, cell polarization and
directed cell migration are reduced but not completely abolished in the absence
of Wnt/PCP signals; this observation indicates that other signaling pathways must
be involved. Results: We show that Phosphoinositide 3-Kinases (PI3Ks) are required
at the onset of zebrafish gastrulation in mesendodermal cells for process formation
and cell polarization. Platelet Derived Growth Factor (PDGF) functions upstream
of PI3K, while Protein Kinase B (PKB), a downstream effector of PI3K activity,
localizes to the leading edge of migrating mesendodermal cells. In the absence
of PI3K activity, PKB localization and cell polarization are strongly reduced
in mesendodermal cells and are followed by slower but still highly coordinated
and directed movements of these cells. Conclusions: We have identified a novel
role of a signaling pathway comprised of PDGF, PI3K, and PKB in the control of
morphogenetic cell movements during gastrulation. Furthermore, our findings provide
insight into the relationship between cell polarization and directed cell migration
at the onset of zebrafish gastrulation.'
acknowledgement: 'We would like to thank Jennifer Geiger, Juan Hurl& Hannu Mansu-koski,
Florian Raible, Marino Zerial, Steve Wilson, and Kurt Anderson for critical reading
of earlier versions of this manuscript. We thank Erez Raz, Bart Vanhaesebroeck,
and Lukas Roth for sending us the pCS2-PH-GFP-nos, the p1IOCAAX, and the pCS2-actin-GFP
constructs, respectively. We are grateful to Marino Zerial and his lab for encouraging
us to start this work and providing us with the dnP13K construct and to Florian
Ulrich and Franziska Friedrich for help with the confocal microscope and artwork,
respectively. We thank Gunter Junghanns and Evelyn Lehmann for excellent fish care.
C.-P.H. is supported by an Emmy-Noother-Fellowship from the Deutsche Forschungsgemeinschaft. '
article_processing_charge: No
article_type: original
author:
- first_name: Juan
full_name: Montero, Juan
last_name: Montero
- first_name: Beate
full_name: Kilian, Beate
last_name: Kilian
- first_name: Joanne
full_name: Chan, Joanne
last_name: Chan
- first_name: Peter
full_name: Bayliss, Peter
last_name: Bayliss
- first_name: Carl-Philipp J
full_name: Heisenberg, Carl-Philipp J
id: 39427864-F248-11E8-B48F-1D18A9856A87
last_name: Heisenberg
orcid: 0000-0002-0912-4566
citation:
ama: Montero J, Kilian B, Chan J, Bayliss P, Heisenberg C-PJ. Phosphoinositide 3-kinase
is required for process outgrowth and cell polarization of gastrulating mesendodermal
cells. Current Biology. 2003;13(15):1279-1289. doi:10.1016/S0960-9822(03)00505-0
apa: Montero, J., Kilian, B., Chan, J., Bayliss, P., & Heisenberg, C.-P. J.
(2003). Phosphoinositide 3-kinase is required for process outgrowth and cell polarization
of gastrulating mesendodermal cells. Current Biology. Cell Press. https://doi.org/10.1016/S0960-9822(03)00505-0
chicago: Montero, Juan, Beate Kilian, Joanne Chan, Peter Bayliss, and Carl-Philipp
J Heisenberg. “Phosphoinositide 3-Kinase Is Required for Process Outgrowth and
Cell Polarization of Gastrulating Mesendodermal Cells.” Current Biology.
Cell Press, 2003. https://doi.org/10.1016/S0960-9822(03)00505-0.
ieee: J. Montero, B. Kilian, J. Chan, P. Bayliss, and C.-P. J. Heisenberg, “Phosphoinositide
3-kinase is required for process outgrowth and cell polarization of gastrulating
mesendodermal cells,” Current Biology, vol. 13, no. 15. Cell Press, pp.
1279–1289, 2003.
ista: Montero J, Kilian B, Chan J, Bayliss P, Heisenberg C-PJ. 2003. Phosphoinositide
3-kinase is required for process outgrowth and cell polarization of gastrulating
mesendodermal cells. Current Biology. 13(15), 1279–1289.
mla: Montero, Juan, et al. “Phosphoinositide 3-Kinase Is Required for Process Outgrowth
and Cell Polarization of Gastrulating Mesendodermal Cells.” Current Biology,
vol. 13, no. 15, Cell Press, 2003, pp. 1279–89, doi:10.1016/S0960-9822(03)00505-0.
short: J. Montero, B. Kilian, J. Chan, P. Bayliss, C.-P.J. Heisenberg, Current Biology
13 (2003) 1279–1289.
date_created: 2018-12-11T12:07:22Z
date_published: 2003-08-05T00:00:00Z
date_updated: 2024-02-27T10:03:37Z
day: '05'
doi: 10.1016/S0960-9822(03)00505-0
extern: '1'
external_id:
pmid:
- ' 12906787'
fulldoi: https://doi.org/10.1016/S0960-9822(03)00505-0
intvolume: ' 13'
issue: '15'
language:
- iso: eng
month: '08'
oa_version: None
page: 1279 - 1289
pmid: 1
publication: Current Biology
publication_identifier:
eissn:
- 1879-0445
issn:
- 0960-9822
publication_status: published
publisher: Cell Press
publist_id: '1950'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Phosphoinositide 3-kinase is required for process outgrowth and cell polarization
of gastrulating mesendodermal cells
type: journal_article
user_id: ea97e931-d5af-11eb-85d4-e6957dddbf17
volume: 13
year: '2003'
...