1. Interaction of a multi-domain adaptor protein, vinexin, with a Rho-effector, Rhotekin
- Author
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Tomiko Asano, Hidenori Ito, Ikuko Iwamoto, Koh-ichi Nagata, and Rika Morishita
- Subjects
Muscle Proteins ,CDC42 ,In Vitro Techniques ,Biology ,SH3 domain ,Cell Line ,Pathology and Forensic Medicine ,Focal adhesion ,GTP-Binding Proteins ,Two-Hybrid System Techniques ,Chlorocebus aethiops ,medicine ,Animals ,Humans ,Protein Interaction Domains and Motifs ,Small GTPase ,Fibroblast ,Molecular Biology ,Adaptor Proteins, Signal Transducing ,Focal Adhesions ,Effector ,Myocardium ,Intracellular Signaling Peptides and Proteins ,Brain ,Colocalization ,Signal transducing adaptor protein ,General Medicine ,Molecular biology ,Recombinant Proteins ,Protein Structure, Tertiary ,Rats ,Cell biology ,medicine.anatomical_structure ,Multiprotein Complexes ,COS Cells ,Apoptosis Regulatory Proteins - Abstract
Among various effector proteins for the Rho small GTPase, the function(s) of Rhotekin is almost unknown. We have identified a multi-domain adaptor protein, vinexin, as a binding partner for Rhotekin, using yeast two-hybrid screening of a human heart library. Rhotekin was found to associate with vinexin in vitro, in COS7 cells, and in brain tissues. The C-terminal Pro-rich motif of Rhotekin exhibited binding to the third SH3 domain of vinexin. The binding was little affected by Rho but was inhibited by activated Cdc42 in COS7 cells. Immunofluorescence analyses revealed partial colocalization of vinexin-alpha with Rhotekin at focal adhesions in REF52 fibroblast cells. These results suggest that Rhotekin forms a complex with vinexin and may play a role at focal adhesions.
- Published
- 2009