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Related Experiment Videos

Tes, a specific Mena interacting partner, breaks the rules for EVH1 binding.

Batiste Boëda1, David C Briggs, Theresa Higgins

  • 1Cell Motility Laboratory, Cancer Research UK, London Research Institute, 44 Lincoln's Inn Fields, London, WC2A 3PX, UK.

Molecular Cell
|December 27, 2007
PubMed
Summary
This summary is machine-generated.

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Tes protein binds to Mena, a member of the Ena/VASP family, through a unique interaction. This binding regulates cell migration by specifically affecting Mena, not other Ena/VASP proteins.

Area of Science:

  • Cell Biology
  • Molecular and Structural Biology
  • Biochemistry

Background:

  • Ena/VASP proteins are crucial cytoskeletal regulators targeted intracellularly via their EVH1 domain binding to FPPPP motifs.
  • Known FPPPP-motif containing proteins include lamellipodin, vinculin, and zyxin, mediating interactions with Ena/VASP proteins.

Purpose of the Study:

  • To investigate the interaction between the Tes protein's LIM3 domain and the EVH1 domain of Ena/VASP family members.
  • To elucidate the structural basis and specificity of the Tes-Mena interaction.
  • To determine the functional consequences of Tes binding on Ena/VASP localization and cell migration.

Main Methods:

  • Structural analysis of the LIM3:EVH1 complex.
  • Structure-based gain-of-function experiments.

Related Experiment Videos

  • In vitro binding assays and cellular localization studies.

    • Main Results:

    • The Tes LIM3 domain binds to the EVH1 domain of Mena, but not VASP or Evl, despite lacking the canonical FPPPP motif.
    • Structural data reveals Tes occludes the FPPPP-binding site, acting as a competitive inhibitor for FPPPP-containing proteins.
    • Tes specifically displaces Mena, but not VASP, from the leading edge and focal adhesions, regulating cell migration via a Mena-dependent pathway.

    Conclusions:

    • Tes is identified as an atypical binding partner for the EVH1 domain, exhibiting specificity for Mena within the Ena/VASP family.
    • The Tes-Mena interaction provides a novel mechanism for regulating cytoskeletal dynamics and cell migration.
    • This study defines a unique mode of interaction and regulation specific to a single Ena/VASP family member.