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Gene Review

Dock1  -  dedicator of cytokinesis 1

Mus musculus

Synonyms: 180 kDa protein downstream of CRK, 9130006G06Rik, AI854900, D630004B07Rik, DOCK180, ...
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Disease relevance of Dock1

  • Netrin promoted the formation of a protein-protein interaction complex that included DOCK180 and the netrin receptor deleted in colorectal carcinoma (DCC) [1].

High impact information on Dock1


Biological context of Dock1

  • We show that a rough-eye phenotype in Drosophila caused by exogenous expression of tyrosine-phosphorylated mouse Dab1RFP is partially rescued by a loss-of-function mutation in myoblast city, a Dock1-like gene in Drosophila [4].

Anatomical context of Dock1


Associations of Dock1 with chemical compounds

  • A novel superfamily of guanine nucleotide exchange factors for Rho GTPases includes DOCK180 and zizimin1 [5].

Physical interactions of Dock1

  • DOCK180 is one of the two principal proteins bound to the SH3 domain of the adaptor protein CrkII [3].

Regulatory relationships of Dock1

  • In a reconstitution experiment, expression of DOCK180 induced hyperphosphorylation of p130(Cas) and a concomitant increase in the amount of CrkII bound to p130(Cas) [3].


  1. Netrin signal transduction and the guanine nucleotide exchange factor DOCK180 in attractive signaling. Li, X., Gao, X., Liu, G., Xiong, W., Wu, J., Rao, Y. Nat. Neurosci. (2008) [Pubmed]
  2. The LIM protein Ajuba influences p130Cas localization and Rac1 activity during cell migration. Pratt, S.J., Epple, H., Ward, M., Feng, Y., Braga, V.M., Longmore, G.D. J. Cell Biol. (2005) [Pubmed]
  3. Evidence that DOCK180 up-regulates signals from the CrkII-p130(Cas) complex. Kiyokawa, E., Hashimoto, Y., Kurata, T., Sugimura, H., Matsuda, M. J. Biol. Chem. (1998) [Pubmed]
  4. Interaction between Dab1 and CrkII is promoted by Reelin signaling. Chen, K., Ochalski, P.G., Tran, T.S., Sahir, N., Schubert, M., Pramatarova, A., Howell, B.W. J. Cell. Sci. (2004) [Pubmed]
  5. Zizimin2: a novel, DOCK180-related Cdc42 guanine nucleotide exchange factor expressed predominantly in lymphocytes. Nishikimi, A., Meller, N., Uekawa, N., Isobe, K., Schwartz, M.A., Maruyama, M. FEBS Lett. (2005) [Pubmed]
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