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Updated: Jun 24, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
Published on: May 26, 2011
Interaction of a multi-domain adaptor protein, vinexin, with a Rho-effector, Rhotekin
Koh-Ichi Nagata1, Hidenori Ito, Ikuko Iwamoto
1Department of Molecular Neurobiology, Institute for Developmental Research, Aichi Human Service Center, 713-8 Kamiya, Kasugai, Aichi, 480-0392, Japan. knagata@inst-hsc.jp
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.
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