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Coupling of PAK-interacting exchange factor PIX to GIT1 promotes focal complex disassembly.

The p21-activated kinase PAK is targeted to focal complexes (FCs) through interactions with the SH3 domains of the PAK-interacting exchange factor PIX and Nck. PIX is a Rac GTP exchange factor that also binds the G-protein-coupled receptor kinase-interacting protein known as GIT1. Overexpression of GIT1 in fibroblasts or epithelial cells causes a loss of paxillin from FCs and stimulates cell motility. This is due to the direct interaction of a C-terminal 125-residue domain of GIT1 with paxillin, under the regulation of PIX. In its activated state, GIT1 can promote FC disassembly independent of actin-myosin contractile events. Additionally, GIT directly couples to a key component of FCs, focal adhesion kinase (FAK), via a conserved Spa2 homology domain. We propose that GIT1 and FAK cooperate to promote motility both by directly regulating focal complex dynamics and by the activation of Rac.

Pubmed ID: 10938112


  • Zhao ZS
  • Manser E
  • Loo TH
  • Lim L


Molecular and cellular biology

Publication Data

September 21, 2000

Associated Grants


Mesh Terms

  • Adaptor Proteins, Signal Transducing
  • Animals
  • COS Cells
  • Cell Cycle Proteins
  • Cell Movement
  • Chickens
  • Cytoskeletal Proteins
  • Cytoskeleton
  • DNA, Complementary
  • Epithelial Cells
  • Fibroblasts
  • Fungal Proteins
  • GTPase-Activating Proteins
  • Glutathione Transferase
  • Guanine Nucleotide Exchange Factors
  • HeLa Cells
  • Humans
  • Microscopy, Phase-Contrast
  • Models, Biological
  • Oncogene Proteins
  • Paxillin
  • Phosphoproteins
  • Plasmids
  • Precipitin Tests
  • Protein Binding
  • Protein Structure, Tertiary
  • Protein-Serine-Threonine Kinases
  • Rho Guanine Nucleotide Exchange Factors
  • Saccharomyces cerevisiae Proteins
  • Signal Transduction
  • Transfection
  • p21-Activated Kinases
  • rac GTP-Binding Proteins
  • src Homology Domains