JCB logo
PeproTech: Cell Culture Supplements
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published 5 December 2005. doi:10.1083/jcb.200507061
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 171, Number 5, 857-869
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 12955K)
Right arrow PPT slides of all figures
Right arrow Supplemental Material Index
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lalli, G.
Right arrow Articles by Hall, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lalli, G.
Right arrow Articles by Hall, A.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

Article

Ral GTPases regulate neurite branching through GAP-43 and the exocyst complex



Giovanna Lalli and Alan Hall

Medical Research Council Laboratory for Molecular Cell Biology and Cell Biology Unit and Department of Biochemistry and Molecular Biology, University College London, London WC1E 6BT, England, UK

Correspondence to Alan Hall: alan.hall{at}ucl.ac.uk

Neurite branching is essential for the establishment of appropriate neuronal connections during development and regeneration. We identify the small GTPase Ral as a mediator of neurite branching. Active Ral promotes neurite branching in cortical and sympathetic neurons, whereas Ral inhibition decreases laminin-induced branching. In addition, depletion of endogenous Ral by RNA interference decreases branching in cortical neurons. The two Ral isoforms, RalA and -B, promote branching through distinct pathways, involving the exocyst complex and phospholipase D, respectively. Finally, Ral-dependent branching is mediated by protein kinase C–dependent phosphorylation of 43-kD growth-associated protein, a crucial molecule involved in pathfinding, plasticity, and regeneration. These findings highlight an important role for Ral in the regulation of neuronal morphology.

Abbreviations used in this paper: cGAP-43, chick GAP-43; EGFP-F, farnesylated EGFP; GAP-43, 43-kD growth-associated protein; GEF, guanine nucleotide exchange factor; PLD, phospholipase D; RNAi, RNA interference; SCG, superior cervical ganglia; siRNA, small interfering RNA.


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 Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?


This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents