Isolation and characterisation of DOCK8, a member of the DOCK180-related regulators of cell morphology

FEBS Lett. 2004 Aug 13;572(1-3):159-66. doi: 10.1016/j.febslet.2004.06.095.


In a yeast two-hybrid system screen for Cdc42-interacting proteins, we identified a protein with similarity to the CrkII-binding protein DOCK180. A cDNA clone of this protein, designated DOCK8, encoded a gene-product of 1701 amino acid residues with a molecular mass of 190 kDa. Immunofluorescence staining showed that transiently transfected HA-tagged DOCK8, as well as endogenous DOCK8, was present at the cell edges in areas undergoing lamellipodia formation. Transient transfection of a C-terminal fragment of DOCK8 resulted in the formation of vesicular structures. Interestingly, these vesicles also contained filamentous actin. These data suggest an involvement of DOCK8 in processes that affect the organisation of filamentous actin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism
  • Amino Acid Sequence
  • Burkitt Lymphoma
  • Cell Line, Tumor
  • Cloning, Molecular
  • DNA, Complementary / genetics
  • Humans
  • Molecular Sequence Data
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Saccharomyces cerevisiae / genetics*
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Signal Transduction
  • Tissue Distribution
  • Transfection
  • rac GTP-Binding Proteins / chemistry
  • rac GTP-Binding Proteins / genetics
  • rac GTP-Binding Proteins / metabolism*
  • rho GTP-Binding Proteins / chemistry
  • rho GTP-Binding Proteins / metabolism


  • Actins
  • DNA, Complementary
  • DOCK1 protein, human
  • Recombinant Proteins
  • rac GTP-Binding Proteins
  • rho GTP-Binding Proteins