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Gene Review

Dok2  -  docking protein 2

Mus musculus

Synonyms: Docking protein 2, Dok-R, Dok-related protein, DokR, Downstream of tyrosine kinase 2, ...
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Disease relevance of Dok2


High impact information on Dok2


Biological context of Dok2


Anatomical context of Dok2

  • Most notably, DokR dramatically reduced repopulation of the thymus, in part by reducing the number of T cell precursors seeding in the thymus, but equally, through inhibiting the transition of CD4(-)CD8(-) to CD4(+)CD8(+) T cells [4].
  • When introduced into lethally irradiated mice, hematopoietic cells expressing DokR showed a drastically reduced capacity to repopulate lymphoid tissues [4].
  • Retroviral-mediated expression of DokR in bone marrow cells dramatically inhibited their capacity to form colonies in vitro in response to the cytokines macrophage colony-stimulating factor and stem cell factor, whereas responses to interleukin-3 and granulocyte macrophage colony-stimulating factor were only weakly affected [4].
  • Dok-R is coexpressed with Tek in a number of endothelial cell lines [6].

Associations of Dok2 with chemical compounds

  • We found that upon ligand binding, CD200R is phosphorylated on tyrosine and subsequently binds to adapter proteins Dok1 and Dok2 [7].
  • Further, they raise the interesting possibility that Dok2 plays an important role in integrin outside-in signaling through a physical and functional interaction with integrin alpha(IIb)beta(3) [8].
  • Background: We previously demonstrated that Dok2 is rapidly phosphorylated on tyrosine residues in platelets in response to thrombin, the immunoreceptor tyrosine-based activation motif-coupled collagen receptor glycoprotein (GP) VI, and by integrin alpha(IIb)beta(3) [8].
  • A unique autophosphorylation site on Tie2/Tek mediates Dok-R phosphotyrosine binding domain binding and function [9].

Physical interactions of Dok2


Regulatory relationships of Dok2


Other interactions of Dok2


Analytical, diagnostic and therapeutic context of Dok2

  • Immunoprecipitation experiments using DokR-specific antibodies revealed an interaction between endogenous DokR and a 150-kDa protein that is tyrosine-phosphorylated in EGF-stimulated BaF/3 cells [5].


  1. Role of Dok-1 and Dok-2 in myeloid homeostasis and suppression of leukemia. Yasuda, T., Shirakata, M., Iwama, A., Ishii, A., Ebihara, Y., Osawa, M., Honda, K., Shinohara, H., Sudo, K., Tsuji, K., Nakauchi, H., Iwakura, Y., Hirai, H., Oda, H., Yamamoto, T., Yamanashi, Y. J. Exp. Med. (2004) [Pubmed]
  2. FRIP, a hematopoietic cell-specific rasGAP-interacting protein phosphorylated in response to cytokine stimulation. Nelms, K., Snow, A.L., Hu-Li, J., Paul, W.E. Immunity (1998) [Pubmed]
  3. Dok-1 and Dok-2 are negative regulators of lipopolysaccharide-induced signaling. Shinohara, H., Inoue, A., Toyama-Sorimachi, N., Nagai, Y., Yasuda, T., Suzuki, H., Horai, R., Iwakura, Y., Yamamoto, T., Karasuyama, H., Miyake, K., Yamanashi, Y. J. Exp. Med. (2005) [Pubmed]
  4. Dok-related protein negatively regulates T cell development via its RasGTPase-activating protein and Nck docking sites. Gugasyan, R., Quilici, C., I, S.T., Grail, D., Verhagen, A.M., Roberts, A., Kitamura, T., Dunn, A.R., Lock, P. J. Cell Biol. (2002) [Pubmed]
  5. Independent SH2-binding sites mediate interaction of Dok-related protein with RasGTPase-activating protein and Nck. Lock, P., Casagranda, F., Dunn, A.R. J. Biol. Chem. (1999) [Pubmed]
  6. The Tek/Tie2 receptor signals through a novel Dok-related docking protein, Dok-R. Jones, N., Dumont, D.J. Oncogene (1998) [Pubmed]
  7. Molecular mechanisms of CD200 inhibition of mast cell activation. Zhang, S., Cherwinski, H., Sedgwick, J.D., Phillips, J.H. J. Immunol. (2004) [Pubmed]
  8. Differential regulation of adapter proteins Dok2 and Dok1 in platelets, leading to an association of Dok2 with integrin alphabeta. Hughan, S.C., Watson, S.P. J. Thromb. Haemost. (2007) [Pubmed]
  9. A unique autophosphorylation site on Tie2/Tek mediates Dok-R phosphotyrosine binding domain binding and function. Jones, N., Chen, S.H., Sturk, C., Master, Z., Tran, J., Kerbel, R.S., Dumont, D.J. Mol. Cell. Biol. (2003) [Pubmed]
  10. Inhibition of the Jun N-terminal protein kinase pathway by SHIP-1, a lipid phosphatase that interacts with the adaptor molecule Dok-3. Robson, J.D., Davidson, D., Veillette, A. Mol. Cell. Biol. (2004) [Pubmed]
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