1. Essential roles of Gab1 tyrosine phosphorylation in growth factor-mediated signaling and angiogenesis
- Author
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Zheng Gen Jin, Meimei Yin, Suowen Xu, and Weiye Wang
- Subjects
Neovascularization, Physiologic ,Protein tyrosine phosphatase ,SH2 domain ,Article ,Receptor tyrosine kinase ,SH3 domain ,chemistry.chemical_compound ,Animals ,Humans ,Medicine ,Phosphorylation ,Adaptor Proteins, Signal Transducing ,biology ,business.industry ,Tyrosine phosphorylation ,Protein-Tyrosine Kinases ,Cell biology ,chemistry ,ROR1 ,biology.protein ,Cancer research ,Intercellular Signaling Peptides and Proteins ,GRB2 ,Cardiology and Cardiovascular Medicine ,business ,Signal Transduction ,Proto-oncogene tyrosine-protein kinase Src - Abstract
Growth factors and their downstream receptor tyrosine kinases (RTKs) mediate a number of biological processes controlling cell function. Adaptor (docking) proteins, which consist exclusively of domains and motifs that mediate molecular interactions, link receptor activation to downstream effectors. 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. Here, we provide an up-to-date overview on the domain structure and biological functions of Gab1, the most intensively studied Gab family protein, in growth factor signaling and biological functions, with a special focus on angiogenesis.
- Published
- 2015