DOCK2
From Wikipedia, the free encyclopedia
Dedicator of cytokinesis 2, also known as DOCK2, is a human gene.[1]
The DOCK2 gene encodes a hematopoietic cell-specific CDM family protein that is indispensable for lymphocyte chemotaxis.[supplied by OMIM][1]
[edit] References
[edit] Further reading
- Reif K, Cyster J (2003). "The CDM protein DOCK2 in lymphocyte migration.". Trends Cell Biol. 12 (8): 368–73. PMID 12191913.
- Nagase T, Seki N, Ishikawa K, et al. (1997). "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain.". DNA Res. 3 (5): 321–9, 341–54. PMID 9039502.
- Nishihara H, Kobayashi S, Hashimoto Y, et al. (1999). "Non-adherent cell-specific expression of DOCK2, a member of the human CDM-family proteins.". Biochim. Biophys. Acta 1452 (2): 179–87. PMID 10559471.
- Fukui Y, Hashimoto O, Sanui T, et al. (2001). "Haematopoietic cell-specific CDM family protein DOCK2 is essential for lymphocyte migration.". Nature 412 (6849): 826–31. doi: . PMID 11518968.
- Brugnera E, Haney L, Grimsley C, et al. (2002). "Unconventional Rac-GEF activity is mediated through the Dock180-ELMO complex.". Nat. Cell Biol. 4 (8): 574–82. doi: . PMID 12134158.
- Nishihara H, Maeda M, Tsuda M, et al. (2002). "DOCK2 mediates T cell receptor-induced activation of Rac2 and IL-2 transcription.". Biochem. Biophys. Res. Commun. 296 (3): 716–20. PMID 12176041.
- Nishihara H, Maeda M, Oda A, et al. (2003). "DOCK2 associates with CrkL and regulates Rac1 in human leukemia cell lines.". Blood 100 (12): 3968–74. doi: . PMID 12393632.
- Côté JF, Vuori K (2003). "Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity.". J. Cell. Sci. 115 (Pt 24): 4901–13. PMID 12432077.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi: . PMID 12477932.
- Sanui T, Inayoshi A, Noda M, et al. (2003). "DOCK2 regulates Rac activation and cytoskeletal reorganization through interaction with ELMO1.". Blood 102 (8): 2948–50. doi: . PMID 12829596.
- Janardhan A, Swigut T, Hill B, et al. (2006). "HIV-1 Nef binds the DOCK2-ELMO1 complex to activate rac and inhibit lymphocyte chemotaxis.". PLoS Biol. 2 (1): E6. doi: . PMID 14737186.
- Brill LM, Salomon AR, Ficarro SB, et al. (2004). "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry.". Anal. Chem. 76 (10): 2763–72. doi: . PMID 15144186.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi: . PMID 15489334.
- Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.". Nat. Biotechnol. 23 (1): 94–101. doi: . PMID 15592455.
- Lu M, Kinchen JM, Rossman KL, et al. (2005). "A Steric-inhibition model for regulation of nucleotide exchange via the Dock180 family of GEFs.". Curr. Biol. 15 (4): 371–7. doi: . PMID 15723800.
- García-Bernal D, Sotillo-Mallo E, Nombela-Arrieta C, et al. (2007). "DOCK2 is required for chemokine-promoted human T lymphocyte adhesion under shear stress mediated by the integrin alpha4beta1.". J. Immunol. 177 (8): 5215–25. PMID 17015707.