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

• Lamellipodia production, or function, is defective and there is a selective reduction in the level and tyrosine phosphorylation of FAK, p130Cas, Crk, and Dock180 at nascent focal complexes [2].
• We found that DOCK180 was phosphorylated and bound to CrkII in NIH 3T3 cells stimulated with integrin and also in 3Y1 cells transformed by v-src or v-crk [3].
• Here, we have studied the involvement of DOCK180 in integrin signaling [3].
• These findings suggest that DOCK180 positively regulates signaling from integrins to CrkII-p130(Cas) complexes at focal adhesions [3].
• Here we identify CrkII, CrkL and Dock1 in complexes bound to tyrosine-phosphorylated Dab1, through mass spectrometry [4].

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

• DOCK180 was neither phosphorylated nor bound to CrkII in quiescent NIH 3T3 cells and 3Y1 cells [3].
• Zizimin2: a novel, DOCK180-related Cdc42 guanine nucleotide exchange factor expressed predominantly in lymphocytes [5].

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].

References