ABSTRACT
The Grb2 associated binder (Gab) adaptor/scaffolding protein family comprises conserved proteins: mammalian Gab1, Gab2 and Gab3, Drosophila Dos and Caenorhabditis elegans Soc1. Gab adaptors are involved in multiple signaling pathways mediated by receptor- and non-receptor protein tyrosine kinases (PTKs), and become phosphorylated upon stimulation by growth factors-, cytokines-, Ig Fc- and antigen receptors. Through its phosphorylated tyrosine containing motifs, proline-rich sequences and pleckstrin homologue (PH) domain Gab adaptors may generate an interacting platform for proteins with SH2 and SH3 domains and may transfer these molecules to the plasma membrane, thereby contributing to their activation. This review will concentrate on the function of mammalian Gab proteins in the signal transduction triggered by immune receptors.
Subject(s)
Adaptor Proteins, Signal Transducing/metabolism , Lymphocytes/immunology , Signal Transduction/immunology , Adaptor Proteins, Signal Transducing/analysis , Adaptor Proteins, Signal Transducing/genetics , Animals , Cell Membrane/chemistry , Cell Membrane/metabolism , Humans , Mice , Phosphorylation , Receptors, Immunologic/metabolismABSTRACT
A cell membrane permeable phosphopeptide corresponding to the SHP-2 binding motif of Grb2-associated binder 1 (Gab1) interferes with the Gab1 adaptor-dependent functions and modulates B cell receptor-triggered intracellular signaling in B cell tumors.
