Frabin and other related Cdc42-specific guanine nucleotide exchange factors couple the actin cytoskeleton with the plasma membrane

J Cell Mol Med. 2008 Aug;12(4):1169-76. doi: 10.1111/j.1582-4934.2008.00345.x. Epub 2008 Apr 9.

Abstract

Frabin, together with, at least, FGD1, FGD2, FGD3 and FGD1-related Cdc42-GEF (FRG), is a member of a family of Cdc42-specific gua-nine nucleotide exchange factors (GEFs). These proteins have multiple phosphoinositide-binding domains, including two pleckstrin homology (PH) domains and an FYVE or FERM domain. It is likely that they couple the actin cytoskeleton with the plasma membrane. Frabin associates with a specific actin structure(s) and induces the direct activation of Cdc42 in the vicinity of this structure(s), resulting in actin reorganization. Furthermore, frabin associates with a specific membrane structure(s) and induces the indirect activation of Rac in the vicinity of this structure(s), resulting in the reorganization of the actin cytoskeleton. This reorganization of the actin cytoskeleton induces cell shape changes such as the formation of filopodia and lamellipodia.

Publication types

  • Review

MeSH terms

  • Actins / metabolism*
  • Amino Acid Sequence
  • Animals
  • Cell Membrane / metabolism*
  • Cytoskeleton / metabolism*
  • Guanine Nucleotide Exchange Factors / chemistry
  • Guanine Nucleotide Exchange Factors / metabolism*
  • Humans
  • Microfilament Proteins / chemistry
  • Microfilament Proteins / genetics
  • Microfilament Proteins / metabolism*
  • Molecular Sequence Data
  • cdc42 GTP-Binding Protein / metabolism*

Substances

  • Actins
  • Guanine Nucleotide Exchange Factors
  • Microfilament Proteins
  • cdc42 GTP-Binding Protein