期刊
FEBS LETTERS
卷 580, 期 12, 页码 455-463出版社
WILEY
DOI: 10.1016/j.febslet.2004.10.110
关键词
Ras; VASP; Mena; actin; lamellipodium; focal adhesion
Ena/VASP family proteins are important modulators of cell migration and localize to focal adhesions, stress fibres and the very tips of lamellipodia and filopodia. Proline-rich proteins like vinculin and zyxin are well established interaction partners, which mediate Ena/VASP-recruitment via their EVH1-domains to focal adhesions and stress fibres. However, it is still unclear, which binding partners Ena/VASP proteins may have at lamellipodia tips and how their recruitment to these cellular protrusions is regulated. Here, we report the identification of a novel protein with high similarity to the C elegans MIG-10 protein, which we termed PREL1 (Proline Rich EVH1 Ligand). PRELI is a 74 kDa protein and shares homology with the Grb7-family of signalling adaptors. We show that PREL1 directly binds to Ena/ VASP proteins and co-localizes with them at lamellipodia tips and at focal adhesions in response to Ras activation. Moreover, PREL1 directly binds to activated Ras in a phosphoinositide-dependent manner. Thus, our data pinpoint PREL1 as the first direct link between Ras signalling and cytoskeletal remodelling via Ena/VASP proteins during cell migration and spreading. (c) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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