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Study shows that growth factor receptor binding protein 2 carboxyl-terminal SH3 domain can bivalently associate with two ligands, in an SH3 dependent manner. Extrapolating the results of this study to the in vivo conditions, Grb2 should bind the SLP65 transducer module first, and then Vav should associate.
Our findings position Grb2 as a key adaptor that integrates various cytokines response in cycling Hematopoietic Stem and Progenitor Cell .
Themis1 acts as a positive regulator of TCR signaling during thymocyte development by promoting Vav1 activity and Grb2 stability
Myogenic differentiation depends on the expression regulation patterns of Grb2 and N-WASP.
Two Dtna interactors, alpha-catulin (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 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 and the TCR complex regulate NF-kappaB via different signaling modules of GRB-2/VAV1 and LAT/ADAP pathways respectively.
GRB2 physically links cyt-PTPe with Src and enables cyt-PTPe to activate Src downstream of activated integrins in osteoclast-like cells.
SUMOylation of Grb2 enhances the ERK activity by increasing its binding with Sos1.
Data indicate that growth factor receptor protein binding protein 2 (Grb2) is upregulated and regulated by Forkhead Box D3 (Foxd3), and pregulated Grb2 interacts with huntingtin (Htt).
Grb2 contributes to immunoreceptor tyrosine-based activation motif signaling in platelets during hemostasis and thrombosis.
Findings indicate Grb2 as a new FAK activator and in coordinating PTPalpha 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.
findings suggest a novel role for GRB2 in ecotropic MLV entry and infection by facilitating mCAT-1 trafficking
study reports that a heterotrimeric protein complex exists between PLD2, Grb2, and WASp in vivo, which is integral to phagocytosis
identify a surprising but pivotal role for dynein and the microtubule network alongside Grb2, Dok-3, and Cbl in antigen gathering during B cell activation
The results suggest that GATA6 is downstream of Grb2 in the inductive signaling pathway and the expression of GATA6 is sufficient to compensate for the defects caused by Grb2 deficiency in the development of the primitive and extraembryonic endoderm.
Ablation of Grb2 in B cells results in enhanced B-cell receptor signaling; however, mutant B cells do not form germinal centers in the spleen after antigen stimulation.
Themis2 was inducibly tyrosine phosphorylated upon LPS challenge and interacted with adaptor protein Grb2 (Q60631).
that miR-1258 can suppress NSCLC progression by targeting the GRB2/Ras/Erk pathway
The binding site of miR-433-3p was identified in the 3'UTR region of GRB2. Western blotting and FQ-PCR showed that miR-433-3p inhibited the mRNA and protein expression of GRB2.
study unravels a unique role of Grb2 in protecting the cytoskeletal architecture in AD-like conditions and presents a potential new strategy for controlling neurodegeneration
M. tuberculosis-initiated human mannose receptor signaling regulates macrophage recognition and vesicle trafficking by gamma Fc receptors, Grb2, and SHP-1.
Data indicate GRB2 as a direct target of miR-329 in pancreatic cancer cells, and expression of GRB2 was inversely correlated with miR-329 expression in pancreatic cancer patients.
EGFR colocalization with GRB2 as assessed by PLA is not correlated with EGFR expression levels or mutation status, defining a patient group that may show EGFR pathway activation, as illustrated by its prognostic value.
Low GRB2 expression is associated with Breast Cancer.
Rab13 activated the downstream AMPK and blocked mTOR signaling by its functional interaction with Grb2 to regulate autophagy in human vascular endothelial cells.
ACTB, CDKN1B, GAPDH, GRB2, RHOA and SDCBP are potent reference genes in neuroendocrine tumors of the lung.
We show that the decrease in PI(4,5)P2 level under non-stimulated conditions inhibits PTEN activity leading to the aberrant activation of the oncoprotein Akt. As well as defining a novel mechanism of Akt phosphorylation with important therapeutic consequences, we also demonstrate that differential expression levels of FGFR2, Plc11 and Grb2 correlate with patient survival
Following phosphorylation of the tyrosine, the proteins growth factor receptor-bound protein 2 (Grb2), Grb2-related adaptor downstream of Shc (Gads), and p85 subunit of phosphoinositide 3-kinase may bind to pYMNM (where pY is phosphotyrosine) via their Src homology 2 (SH2) domains, leading to downstream signaling to distinct immune pathways. These three adaptor proteins bind to the same site on CD28 with variable affinity
investigated the target and mechanism of miR-411-5p in breast cancer using mimic and inhibitor, and demonstrated the involvement of GRB2 and Ras activation
The study presents EPR 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 induces Grb2 to recruit PI3-K to TGF-RII that activates JNK/AP-1-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 signalling. The dimeric state is inhibitory to this process. The self-association/dissociation of Grb2 represents a switch that regulates MAP kinase 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 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 and this interaction being stronger could replace Gab1, with mutant Htt becoming the preferred partner. This would have immense effect on downstream signaling events.
in VSMCs exposed to hyperglycemia, IGF-I stimulation of Shc facilitates the transfer of Grb2 to p85 resulting in enhanced PI3K activation and AKT 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