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Papers In Press, published online ahead of print February 26, 2002
Pharmacology, NYU School of Medicine, New York, NY 10016
Corresponding Author: jan.sap{at}med.nyu.edu
SRC family kinases have been consistently and recurrently implicated in neurite extension events, yet the mechanism underlying their neuritogenic role has remained elusive. We report that EGF can be converted from a non-neuritogenic into a neuritogenic factor through moderate activation of endogenous SRC by RPTP
J. Biol. Chem, 10.1074/jbc.M111902200
Submitted on December 13, 2001
Revised on February 20, 2002
Accepted on February 26, 2002
c-SRC mediates neurite outgrowth through recruitment of Crk to the scaffolding protein Sin/Efs, without altering the kinetics of ERK activation
(a physiological SRC activator). We show that such a qualitative change in the response to EGF is not accompanied by changes in the extent or kinetics of ERK induction in response to this factor. Instead, the pathway involved relies on increased tyrosine phosphorylation of, and recruitment of Crk to, the SRC substrate Sin/Efs. The latter is a scaffolding protein structurally similar to the SRC substrate p130cas, tyrosine phosphorylation of which is critical for migration in fibroblasts and epithelial cells. Expression of a dominant negative version of Sin interfered with RPTP/EGF- as well as FGF-induced neurite outgrowth. These observations uncouple neuritogenic signaling in PC12 cells from sustained activation of ERK kinases, and for the first time identify an effector of SRC's function in neurite extension.
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