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Related Experiment Videos

Abl kinase interacts with and phosphorylates vinexin.

Masaru Mitsushima1, Honami Takahashi, Tomoyuki Shishido

  • 1Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.

FEBS Letters
|July 13, 2006
PubMed
Summary

Vinexin alpha and beta interact with c-Abl, localizing to membrane ruffles. Vinexin alpha is phosphorylated by Abl, suggesting it

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Area of Science:

  • Cell biology
  • Molecular biology
  • Biochemistry

Background:

  • Non-receptor tyrosine kinase Abl regulates the actin cytoskeleton, stress fibers, and membrane ruffles.
  • Vinexin is an adapter protein with three SH3 domains, involved in signal transduction and actin cytoskeleton reorganization.

Purpose of the Study:

  • To investigate the interaction between vinexin and c-Abl.
  • To identify the role of vinexin in Abl-mediated signaling.
  • To determine if vinexin is a substrate for Abl.

Main Methods:

  • Co-immunoprecipitation to study protein interactions.
  • Immunofluorescence microscopy to observe protein colocalization.
  • Treatment with latrunculin B to assess F-actin involvement.
  • Site-directed mutagenesis to identify phosphorylation sites.

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Main Results:

  • Vinexin alpha and beta interact with c-Abl via the third SH3 domain.
  • Vinexin and c-Abl colocalize at membrane ruffles in rat astrocytes.
  • The interaction is reduced by latrunculin B, indicating F-actin mediation.
  • Vinexin alpha, but not beta, is tyrosine phosphorylated upon co-expression with c-Abl or v-Abl.
  • Tyrosine 127 on vinexin alpha is a major phosphorylation site by Abl.

Conclusions:

  • Vinexin alpha and beta interact with c-Abl in an F-actin-dependent manner.
  • Vinexin alpha is a novel substrate for Abl, with tyrosine 127 being a key phosphorylation site.