Cdc42 GTPase-activating protein (CdGAP) interacts with the SH3D domain of Intersectin through a novel basic-rich motif

FEBS Lett. 2011 Mar 23;585(6):847-53. doi: 10.1016/j.febslet.2011.02.022. Epub 2011 Feb 22.

Abstract

The small GTPases Rac1 and Cdc42 are key regulators of the cytoskeleton. We have previously identified the endocytic protein Intersectin as a binding partner and regulator of Cdc42 GTPase-activating protein (CdGAP) with activity towards Rac1 and Cdc42. This interaction is mediated through the SH3D domain of Intersectin and the central domain of CdGAP, which does not contain any typical proline-rich domain or known SH3-binding motif. Here, we have characterized the Intersectin-SH3D/CdGAP interaction. We show that Intersectin-SH3D interacts directly with a small region of CdGAP highly enriched in basic residues and comprising a novel conserved xKx(K/R)K motif.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Vesicular Transport / genetics
  • Adaptor Proteins, Vesicular Transport / metabolism*
  • Amino Acid Motifs*
  • Amino Acid Sequence
  • Animals
  • Blotting, Western
  • GTPase-Activating Proteins / genetics
  • GTPase-Activating Proteins / metabolism*
  • HEK293 Cells
  • Humans
  • Immunoprecipitation
  • Mice
  • Molecular Sequence Data
  • Mutation
  • Protein Binding
  • Sequence Homology, Amino Acid
  • src Homology Domains*

Substances

  • Adaptor Proteins, Vesicular Transport
  • Arhgap31 protein, mouse
  • GTPase-Activating Proteins
  • intersectin 1