spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search    

The fully linked HTML version of this article has now been published.
Development ePress online publication date 23 Feb 2005
doi: 10.1242/dev.01703

This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
dev.01703v1
132/7/1511    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Liu, K. J.
Right arrow Articles by Harland, R. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Liu, K. J.
Right arrow Articles by Harland, R. M.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

Research article

Inhibition of neurogenesis by SRp38, a neuroD-regulated RNA-binding protein


Karen J. Liu and Richard M. Harland*
* Author for correspondence (e-mail: harland{at}socrates.berkeley.edu)

Although serine-arginine rich (SR) proteins have often been implicated in the positive regulation of splicing, recent studies have shown that one unusual SR protein, SRp38, serves, contrastingly, as a splicing repressor during mitosis and stress response. We have identified a novel developmental role for SRp38 in the regulation of neural differentiation. SRp38 is expressed in the neural plate during embryogenesis and is transcriptionally induced by the neurogenic bHLH protein neuroD. Overexpression of SRp38 inhibits primary neuronal differentiation at a step between neurogenin and neuroD activity. This repression of neuronal differentiation requires activation of the Notch pathway. Conversely, depletion of SRp38 activity results in a dysregulation of neurogenesis. Finally, SRp38 can interact with the peptidyltransferase center of 28S rRNA, suggesting that SRp38 activity may act, in part, via regulation of ribosome biogenesis or function. Strikingly, recent studies of several cell cycle regulators during primary neurogenesis have also revealed a crucial control step between neurogenin and neuroD. SRp38 may mediate one component of this control by maintaining splicing and translational silencing in undifferentiated neural cells.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?


This article has been cited by other articles:


Home page
 DevelopmentHome page
H. Takada, T. Kawana, Y. Ito, R. F. Kikuno, H. Mamada, T. Araki, H. Koga, M. Asashima, and M. Taira
The RNA-binding protein Mex3b has a fine-tuning system for mRNA regulation in early Xenopus development
Development, July 15, 2009; 136(14): 2413 - 2422.
[Abstract] [Full Text] [PDF]

Home page
 JCBHome page
P. Bjork, S. Jin, J. Zhao, O. P. Singh, J.-O. Persson, U. Hellman, and L. Wieslander
Specific combinations of SR proteins associate with single pre-messenger RNAs in vivo and contribute different functions
J. Cell Biol., February 23, 2009; 184(4): 555 - 568.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
L. Marin-Vinader, C. Shin, C. Onnekink, J. L. Manley, and N. H. Lubsen
Hsp27 Enhances Recovery of Splicing as well as Rephosphorylation of SRp38 after Heat Shock
Mol. Biol. Cell, February 1, 2006; 17(2): 886 - 894.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
C. Shin, F. E. Kleiman, and J. L. Manley
Multiple Properties of the Splicing Repressor SRp38 Distinguish It from Typical SR Proteins
Mol. Cell. Biol., September 15, 2005; 25(18): 8334 - 8343.
[Abstract] [Full Text] [PDF]


© The Company of Biologists Ltd 2005