Anti-phospho Gab2 (Thr391) Antibody

Grb2-associated binder (Gab) proteins serve as docking proteins, recruiting SH2 domain-containing effectors and relaying signals to downstream signalling pathways from receptor tyrosine kinases (RTKs) such as growth factor, cytokine and antigen receptors.  There are three mammalian Gab proteins, Gab1-3.  These all contain Grb2 SH3 domain-binding sites and multiple tyrosine phosphorylation sites.  Following tyrosine phosphorylation, Gab proteins recruit the tyrosine phosphatase SHP2 and the p85 subunit of pI3K, resulting in potentiation of the Ras/Erk and PI3K/Akt pathways.
Gab proteins are also subject to negative regulation.  It has recently been demonstrated that growth factor-induced phosphorylation of Gab2 on Ser210 and Thr391 leads to the recruitment of 14-3-3 proteins which promotes dissociation of Gab2 from Grb2.  Gab2 is thus uncoupled from the receptor complex, resulting in termination of Gab2 signalling (1).  This regulatory mechanism is unique to Gab2.

(1) Brummer, T. et al.  EMBO J. (2008) 27; 1-12.