IndraLab
Statements
"In this study, we describe the specific interaction of PAK1 with the Grb2 adapter protein both in vitro and in vivo. We identify the site of this interaction as the second proline-rich SH3 binding domain of PAK1. Stimulation of the epidermal growth factor receptor (EGFR) in HaCaT cells enhances the level of EGFR-associated PAK1 and Grb2, although the PAK1-Grb2 association is itself independent of this stimulation. "
"The dimerization of two EGFR family molecules leads to phosphorylation of C-terminal tyrosine residues either by autophosphorylation or by a SRC-related kinase followed by binding of GRB2, a RAS adaptor protein, at the SH2 domain of the receptor; binding of the proline-rich C-terminus of SOS, a guanine nucleotide exchange factor, to the SH3 domain of the receptor; exchange of a GTP from the receptor complex for a GDP from the RAS protein to form activated RAS; activation of phosphatidylinositol-3-kinase (PI-3 kinase) to initiate signaling by the biochemical pathways that are triggered by diacylglycerol production and protein kinase C activation; and activation of the series of cytoplasmic serine and threonine kinases beginning with RAF to initiate signaling by the biochemical pathways that are triggered by members of the MAPK family (e.g. ERK 1 and 2). EGFR signaling also activates other pathways in the cell including the Janus kinase (JAK)/signal transduction activators of transcription (STAT) pathways [80, 81]."