QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

First published online 10 July 2007
doi: 10.1242/jcs.003657

This Article Figures Only Full Text Full Text (PDF) Supplementary Material All Versions of this Article: jcs.003657v1 120/15/2555    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Sandilands, E. Articles by Frame, M. C. Search for Related Content PubMed PubMed Citation Articles by Sandilands, E. Articles by Frame, M. C. Social Bookmarking                         What's this?

The membrane targeting and spatial activation of Src, Yes and Fyn is influenced by palmitoylation and distinct RhoB/RhoD endosome requirements

The Beatson Institute for Cancer Research, Cancer Research UK Beatson Laboratories, Garscube Estate, Switchback Road, Bearsden, Glasgow, G61 1BD, UK

^* Author for correspondence (e-mail: m.frame{at}beatson.gla.ac.uk)

Accepted 29 May 2007

Src activation is a tightly regulated process which requires RhoB endosome-associated actin assembly and transit to the cell periphery. We show here that although two other ubiquitous Src family kinases (SFKs) Yes and Fyn also require intact actin filaments for peripheral membrane targeting, they display distinct spatial activation and endosomal requirements. Unlike Src, both Yes and Fyn are constitutively membrane-localized to some extent, and Fyn is present in RhoD-positive endosomes whereas Yes does not visibly colocalize with either of the endosomal markers RhoB or RhoD. By modulating amino acid acceptor sites for palmitoylation in Src, Yes and Fyn, we show that Src S3C/S6C, which is palmitoylated (unlike wild-type Src) behaves in a manner more similar to Fyn, by predominantly colocalizing with RhoD endosomes, and the targeting of both Fyn and Src S3C/S6C is inhibited by siRNA-mediated knockdown of RhoD. Moreover, Fyn C3S/C6S, which is no longer palmitoylated, behaves much more like Src by colocalizing with RhoB endosomes and by requiring RhoB for activation and membrane translocation. These data imply that distinct modes of spatial activation and membrane delivery, at least partly under the control of specific acylation attachment sequences and endosome sub-type requirements, define distinct properties of the three ubiquitously expressed SFKs.

Key words: Actin, RhoB, Src

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    Twitter    What's this?

This article has been cited by other articles:

				M.-C. Landry, A. Sicotte, C. Champagne, and J. N. Lavoie Regulation of Cell Death by Recycling Endosomes and Golgi Membrane Dynamics via a Pathway Involving Src-family kinases, Cdc42 and Rab11a Mol. Biol. Cell, September 15, 2009; 20(18): 4091 - 4106. [Abstract] [Full Text] [PDF]

				K. Tsutsumi, M. Tomomura, T. Furuichi, and S.-i. Hisanaga Palmitoylation-dependent endosomal localization of AATYK1A and its interaction with Src Genes Cells, September 1, 2008; 13(9): 949 - 964. [Abstract] [Full Text] [PDF]

				G. A. Knock, Y. Shaifta, V. A. Snetkov, B. Vowles, S. Drndarski, J. P.T. Ward, and P. I. Aaronson Interaction between src family kinases and rho-kinase in agonist-induced Ca2+-sensitization of rat pulmonary artery Cardiovasc Res, February 1, 2008; 77(3): 570 - 579. [Abstract] [Full Text] [PDF]