Document Detail


The membrane targeting and spatial activation of Src, Yes and Fyn is influenced by palmitoylation and distinct RhoB/RhoD endosome requirements.
MedLine Citation:
PMID:  17623777     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Emma Sandilands; Valerie G Brunton; Margaret C Frame
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2007-07-10
Journal Detail:
Title:  Journal of cell science     Volume:  120     ISSN:  0021-9533     ISO Abbreviation:  J. Cell. Sci.     Publication Date:  2007 Aug 
Date Detail:
Created Date:  2007-07-24     Completed Date:  2007-12-06     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0052457     Medline TA:  J Cell Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  2555-64     Citation Subset:  IM    
Affiliation:
The Beatson Institute for Cancer Research, Cancer Research UK Beatson Laboratories, Garscube Estate, Switchback Road, Bearsden, Glasgow, G61 1BD, UK.
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MeSH Terms
Descriptor/Qualifier:
Actins / isolation & purification,  metabolism*
Animals
Cell Line
Cell Membrane / metabolism
Endocytosis
Endosomes / metabolism*
Gene Expression Regulation
Genes, src
Mice
Palmitic Acid / metabolism
Proto-Oncogene Proteins c-fyn / metabolism*
Proto-Oncogene Proteins c-yes / metabolism*
Proto-Oncogene Proteins pp60(c-src) / isolation & purification,  metabolism*
rho GTP-Binding Proteins / isolation & purification,  metabolism*
rhoB GTP-Binding Protein / isolation & purification,  metabolism*
Chemical
Reg. No./Substance:
0/Actins; 57-10-3/Palmitic Acid; EC 2.7.10.1/Proto-Oncogene Proteins c-yes; EC 2.7.10.2/Proto-Oncogene Proteins c-fyn; EC 2.7.10.2/Proto-Oncogene Proteins pp60(c-src); EC 3.6.1-/Rhod protein, mouse; EC 3.6.5.2/rho GTP-Binding Proteins; EC 3.6.5.2/rhoB GTP-Binding Protein

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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