Apr 1, 2021 · Grb2 forms a bidentate interaction with both the N-terminal SH2 and the catalytic domains of Shp2, releasing the phosphatase from its auto-inhibited conformation. Grb2 typically exists as a...

Jun 6, 2002 · The SH2 domain of Grb2 directly recognizes phospho-tyrosine-containing sites on a number of tyrosine kinases and tyrosine kinase receptors. The Grb2 SH3 domains bind to the Ras guanine nucleotide exchange factor Sos, thereby linking Grb2 recruitment to Ras activation (8–10). Importantly, this Grb2-dependent Ras activation pathway has been ...

Overexpression of truncated SHP-2 that lacks Grb2-interacting sites, but not the full-length catalytically inactive SHP-2, reduces ERK activation by IL-6, confirming the signal-mediating role of SHP-2. Activation of ERK1/2 is correlated with induction of …

Dec 1, 2000 · SHP-2, a cytoplasmic SH2 domain containing protein tyrosine phosphatase, is involved in the signaling pathways of a variety of growth factors and cytokines.

We propose that SHP-2 plays a pivotal role in FGFR signaling in myoblasts via both Erk-dependent and Erk-independent pathways. Cell lines of the myogenic lineage provide an excellent model for studying signaling pathways that …

Nov 19, 1998 · Using a tyrosine-phosphorylated GST-G-CSF-R fusion we demonstrate that Shc, Grb2 and SHP-2 directly bind the receptor via their respective SH2 domains, suggesting multiple routes of MAPK activation from the G-CSF-R are possible.

A positive role for SHP-2 as a regulator of the Erk pathway has been proposed based on the observation that SHP-2 is phosphorylated on tyrosine residues in response to PDGF. This provides a binding site for the Grb2 adapter protein and hence the ability to form a SHP-2/Grb2/SOS complex with potential to activate the Ras pathway .

SHP-2 (also named PTP1D, syp, or SH-PTP2) has been identified as a phosphotyrosine phosphatase comprising two src-homology-2 (SH2) domains. Upon growth factor stimulation, SHP-2 becomes tyrosine phosphorylated, thereby increasing its catalytic activity.

Apr 1, 2021 · Grb2 forms a bidentate interaction with both the N-terminal SH2 and the catalytic domains of Shp2, releasing the phosphatase from its auto-inhibited conformation. Grb2 typically exists as a dimer in the cytoplasm.

Feb 11, 2025 · SHP-2 modulates multiple signaling cascades by dephosphorylating key regulatory proteins. In the Ras/MAPK cascade, it influences cell growth and differentiation by removing phosphate groups from substrates like GRB2. SHP-2 acts as a molecular switch, toggling pathways in response to stimuli.