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Human GRB2 Protein expressed in Escherichia coli (E. coli) - ABIN667098
Weisswange, Newsome, Schleich, Way: The rate of N-WASP exchange limits the extent of ARP2/3-complex-dependent actin-based motility. in Nature 2009
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Two Dtna (show DTNA Proteins) interactors, alpha-catulin (show CTNNAL1 Proteins) (phosphorylation independent) and Grb2 (phosphorylation dependent) are localized to neuromuscular junctions in vivo, and are required for proper organization of neurotransmitter receptors on myotubes.
Grb2-deficient T cells show defects in T cell development, increased Th1 (show HAND1 Proteins) and Th17 cell differentiation capacities, and impaired proliferation after activation by dendritic cells, which likely reduce the clinical symptoms of EAE.
provide evidence that CD28 (show CD28 Proteins) and the TCR complex regulate NF-kappaB (show NFKB1 Proteins) via different signaling modules of GRB-2/VAV1 (show VAV1 Proteins) and LAT (show LAT Proteins)/ADAP (show APP Proteins) pathways respectively.
GRB2 physically links cyt (show CYGB Proteins)-PTPe (show PTPRE Proteins) with Src (show SRC Proteins) and enables cyt (show CYGB Proteins)-PTPe (show PTPRE Proteins) to activate Src (show SRC Proteins) downstream of activated integrins in osteoclast-like cells.
SUMOylation of Grb2 enhances the ERK (show EPHB2 Proteins) activity by increasing its binding with Sos1 (show SOS1 Proteins).
Data indicate that growth factor receptor (show RYK Proteins) protein binding protein 2 (Grb2) is upregulated and regulated by Forkhead Box D3 (Foxd3 (show FOXD3 Proteins)), and pregulated Grb2 interacts with huntingtin (Htt (show HTT Proteins)).
Grb2 contributes to immunoreceptor tyrosine-based activation motif signaling in platelets during hemostasis and thrombosis.
Findings indicate Grb2 as a new FAK (show PTK2 Proteins) activator and in coordinating PTPalpha (show PTPRA Proteins) tyrosine phosphorylation to enable downstream integrin signaling and migration.
Grb2 is not required for the establishment of the glomerular filtration barrier in vivo.
Study shows that the ability of Sos1/Grb2 to appropriately regulate pluripotency and differentiation factors and to initiate primitive endoderm development requires collective binding of multiple Sos1/Grb2 domains to their protein and phospholipid ligands.
The study presents EPR (show EREG Proteins) spectroscopic analysis of the binding of the wild-type and mutant Grb2 SH2 domains to the CSpYVNVQC peptide variant. These data confirm that the binding specificity of SH2 domains, even that of Grb2, results from multiple factors and does not depend merely on the nature of one particular residue.
TGF-beta2 (show TGFB2 Proteins) induces Grb2 to recruit PI3-K (show PIK3CA Proteins) to TGF-RII that activates JNK (show MAPK8 Proteins)/AP-1 (show FOSB Proteins)-signaling and augments invasiveness of Theileria-transformed macrophages.
Genetic variation near GRB2 on chromosome 17q25.1 is associated with sight-threatening diabetic retinopathy.
Only monomeric Grb2 is capable of upregulating MAP kinase (show MAPK1 Proteins) signalling. The dimeric state is inhibitory to this process. The self-association/dissociation of Grb2 represents a switch that regulates MAP kinase (show MAPK1 Proteins) activity and hence controls cancer progression.
The immunoglobulin tail tyrosine motif in the cytoplasmic segments of membrane-bound IgGs acts as the principle signal amplifier by incorporating a Grb2-Btk (show BTK Proteins) signaling.
findings show that regions outside of the consensus PxxPxR sites drive the high affinity association of GRB2 with SH3 domain ligands
down-regulated molecule growth factor receptor-bound protein 2 (GRB2) was a prominent node in fourteen cell proliferation-related sub-pathways.
C-SH3 of Grb2 mediates the interaction with mutant Htt (show HTT Proteins) and this interaction being stronger could replace Gab1, with mutant Htt (show HTT Proteins) becoming the preferred partner. This would have immense effect on downstream signaling events.
GRB2 was an independent factor in prognosis of esophageal squamous cell carcinoma patients
In addition, GRB2 and UBC (show RPS27A Proteins) were found to be hub nodes in the differentially expressed subnetwork and may be used as potential biomarkers or targets for the diagnosis of bladder cancer.
in VSMCs exposed to hyperglycemia, IGF-I (show IGF1 Proteins) stimulation of Shc (show SHC1 Proteins) facilitates the transfer of Grb2 to p85 (show ARHGEF7 Proteins) resulting in enhanced PI3K activation and AKT (show AKT1 Proteins) phosphorylation leading to enhanced cell proliferation and migration
The protein encoded by this gene binds the epidermal growth factor receptor and contains one SH2 domain and two SH3 domains. Its two SH3 domains direct complex formation with proline-rich regions of other proteins, and its SH2 domain binds tyrosine phosphorylated sequences. This gene is similar to the Sem5 gene of C.elegans, which is involved in the signal transduction pathway. Two alternatively spliced transcript variants encoding different isoforms have been found for this gene.
growth factor receptor-bound protein 2
, Growth factor receptor-bound protein 2
, SH2/SH3 adapter GRB2
, adapter protein GRB2
, protein Ash
, abundant SRC homology
, epidermal growth factor receptor-binding protein GRB2
, growth factor receptor-bound protein 3
, growth factor receptor bound protein 2