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The suppressor of cytokine signaling (SOCS)-7 interacts with the actin cytoskeleton through vinexin

par Martens, Nele;Hooghe, Robert;Peters, Elisabeth ;Wery, Maxime ;Vandenhaute, Jean;Wang, Ping;Braet, Filip;Gertler, Arieh
Référence Experimental cell research, 298, 1, page (239-248)
Publication Publié, 2004-08

Article révisé par les pairs

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Résumé :

To understand the function of the suppressor of cytokine signaling (SOCS)-7, we have looked for proteins interacting with SOCS-7 in a stringent yeast two-hybrid screen of a human leukocyte cDNA-library. We identified the cytoskeletal molecule vinexin as a partner interacting with SOCS-7. Tests with deletion mutants of SOCS-7 demonstrated that a central region of the molecule containing several proline-rich regions, N-terminal to the SH2 domain, was responsible for the binding to vinexin. It is thus likely that one of the SH3 domains of vinexin interacts with a poly-proline region of SOCS-7. The interaction with vinexin was confirmed biochemically as vinexin-α was co-precipitated with SOCS-7. Confocal laser-scanning microscopy in HEK293T, MCF-7, and 3T3-L1 cells showed that part of the transfected SOCS-7-green fluorescent protein (GFP) molecules merged with vinexin and with actin. Taken together, our data indicate that SOCS-7 interacts with vinexin and the actin cytoskeleton. © 2004 Elsevier Inc. All rights reserved.