Biochemical and Biophysical Research Communications
Regular ArticleUnique Phosphorylation Mechanism of Gab1 Using PI 3-Kinase as an Adaptor Protein
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Cited by (5)
The involvement of the docking protein Gab1 in mitogenic signalling induced by EGF and HGF in rat hepatocytes
2013, Biochimica et Biophysica Acta - Molecular Cell ResearchCitation Excerpt :Activated Met has also been found to recruit a complex of Gab1/Grb2/SHP-2, leading to stimulation of the Ras/ERK pathway [33]. PI3K can be recruited directly to the multisubstrate docking site of Met or indirectly through Gab1 [34,35]. The relationship between, and relative importance of, Gab1 and Shc in Met signalling has been a matter of debate [22,36–38].
Regulation of TRPC6 Channel Activity by Tyrosine Phosphorylation
2004, Journal of Biological ChemistryCitation Excerpt :The Fyn-TRPC6 interaction is mediated by the SH2 domain of Fyn and the NH2-terminal cytoplasmic domain of TRPC6; this interaction is not dependent on phosphorylation. Although associations involving the SH2 domain are usually mediated by an SH2-phosphotyrosine-based interaction, a phosphorylation-independent interaction between the SH2 domain and its target proteins has been reported in several SH2-dependent protein interactions (36, 38–40). TRPC6 might also recruit other SH2-containing signaling molecules in the macromolecular signaling complex to maintain proper TRPC6 channel regulation via the NH2-terminal cytoplasmic domain.
Neurotrophins in the regulation of cellular survival and death
2014, Handbook of Experimental Pharmacology
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