Doks are a family of adaptor proteins that recruit SH2-containing molecules involved in various cell signaling pathways. Six Dok proteins (Dok1 to Dok6) have been identified and each has an N-terminal pleckstrin homology domain, a central phosphotyrosine binding domain, and a C-terminal region containing multiple tyrosine residues. When phosphorylated, these tyrosines can serve as docking sites for SH2 domain-containing proteins. Dok1 (p62dok) has been shown to bind Ras-GAP, Nck, and Csk. Several tyrosine phosphorylation sites have been identified for Dok1. One site, Tyr-362 (Tyr-361 mouse), is phosphorylated by c-Abl, is required for Nck binding, and may be critical for filopodia formation during fibroblast spreading on fibronectin. Alternatively, Dok1 activity is also regulated by serine phosphorylation. IκB Kinase β phosphorylates several serine sites including Ser-450 in vitro, and TNFα, IL-1, and radiation treatment lead to phosphorylation of Ser-443, Ser-446, and Ser-450 in vivo. Phosphorylation of these serine sites may be required for Dok-mediated inhibition of MAPK signaling and stimulation of cell motility.
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Kashige, N. et al. (2000) Proc. Nat. Acad. Sci. 97(5):2093.
Noguchi, T. et al. (1999) EMBOJ 18(7):1748.
*For more information, see UniProt Accession Q99704
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
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