Structure and function of Gab2 and its role in cancer (Review).
Zunyi, China. In Mol Med Report, Sep 2015
Gab2 protein lacks intrinsic catalytic activity; however, when phosphorylated by protein‑tyrosine kinases (PTKs), Gab2 recruits several Src homology‑2 (SH2) domain‑containing proteins, including the SH2‑containing protein tyrosine phosphatase 2 (SHP2), the p85 subunit of phosphoinositide‑3 kinase (PI3K), phospholipase C‑γ (PLCγ)1, Crk, and GC‑GAP.
Essential roles of Gab1 tyrosine phosphorylation in growth factor-mediated signaling and angiogenesis.
Rochester, United States. In Int J Cardiol, Mar 2015
Recent studies have revealed that Grb2-associated-binders (Gab) family members (including Gab1, Gab2, and Gab3), when phosphorylated on tyrosine residues, provide binding sites for multiple effector proteins, such as Src homology-2 (SH2)-containing protein tyrosine phosphatase 2 (SHP2) and phosphatidylinositol 3-kinase (PI3K) regulatory subunit p85, thereby playing important roles in transducing RTKs-mediated signals into pathways with diversified biological functions.
The double life of p85.
United States. In Cancer Cell, 2014
A growing number of mutations in PIK3R1, the gene that encodes for the p85α regulatory subunit of PI3K, have been recently identified.
The structural basis for cancer treatment decisions.
More papers using
Tel Aviv-Yafo, Israel. In Oncotarget, 2014
Examples include redundant pathways taking over after inhibition of EGFR constitutive activation, mutations in PIK3CA p110α and p85, and the non-hotspot AKT1 mutants conferring constitutive membrane localization.