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. Author manuscript; available in PMC: 2017 Jan 7.
Published in final edited form as: Mol Cell. 2015 Dec 10;61(1):98–110. doi: 10.1016/j.molcel.2015.11.010

Figure 6. Mutations of PLCγ residues that interface with the “phosphorylating” kinase impair PLCγ phosphorylation without impacting PLCγ recruitment to the FGFR, PDGFR and VEGFR.

Figure 6

(A) Gln-677 and Glu-762 of PLCγ and the phosphotyrosine binding pocket of cSH2 domain lie on the opposing faces of cSH2 domain. (B–D) PLCγ null fibroblasts were transfected with expression vectors for wild-type PLCγ, and the indicated PLCγ mutants. Following cell stimulation with 50 ng/ml FGF1, PDGF or VEGF, cell lysates were blotted with the indicated antibodies. See also Figure S7.