2024年9月1日 · GRB2, or Growth Factor Receptor-Bound Protein 2, is a pivotal adaptor protein in intracellular signal transduction pathways, particularly within receptor tyrosine kinase (RTK) signaling cascades.

These experiments provide direct biochemical evidence that binding to the IL-2R of the adaptor protein Shc requires phosphorylation of Tyr-338 in the IL-2Rbeta acidic subdomain. In addition, we report that STAT proteins that are activated by IL-2, i.e. STAT1, STAT3 and STAT5, indeed associate with the IL-2Rbeta chain.

2009年9月18日 · We found that hPIV3-C interacts directly through its C-terminal domain with STAT1 and GRB2, whereas C proteins from measles or Nipah viruses failed to do so. Binding to STAT1 explains the previously reported capacity of hPIV3-C to block type I interferon signaling, but the interaction with GRB2 was unexpected.

stat1参与控制细胞生长、增强血管形成和诱导细胞死亡，这些功能都呈现抑制肿瘤生长的特征。 小结一下（如下图），不同的配合、受体，对应不同的JAK二聚物组合，最终可以将信号传导给不同的STAT蛋白，从而激活不同的下游通路。

2003年12月1日 · In the present study, we report that transient expression of Grb2 specifically down-regulates EGF-stimulated tyrosine phosphorylation of Stat3, which leads to a repression of Stat3 transcriptional activity. In contrast, depletion of Grb2 by RNA interference substantially increases Stat3 tyrosine phosphorylation induced by EGF.

2009年9月18日 · (D) GRB2 and STAT1 compete for hPIV3-C binding. GST alone (line 1) or GST-tagged hPIV3-C (line 2–6; 300 ng/well in a 6-well plate) were expressed in HEK-293T cells together with 600 ng/well (line 3–4; “++”) or 150 ng/well (line 5–6; “+”) of 3×-FLAG-tagged STAT1 and/or 3×-FLAG-tagged GRB2 (line 2, 3 and 5; 600 ng/well).

2024年11月1日 · Here, we present the biophysical characterization of Grb2 Y160F, the first Grb2 mutant to induce protein monomerization without disrupting its native behavior in solution due to net charge modifications or interaction with peptides. We also identified that Grb2 Y160F exists in a monomer-dimer equilibrium.

Grb2 (growth factor receptor-binding protein 2) is a small adaptor protein with no catalytic activity. Comprising only one SH2 domain surrounded by two SH3 domains, Grb2 direct complex formation with proline-rich regions of other proteins through its two SH3 domains and binds phosphotyrosine sites of other proteins through its SH2 domain.

GRB2-associated binding protein 1 (GAB1) is recruited to phosphorylated FRS2, where it is phosphorylated and also recruits PI3K to activate PI3K-AKT signaling . PI3K-AKT signaling downstream of FGFR activation is involved in FGF-mediated angiogenesis [56,57] and negatively regulates ERK1/2 signaling .

2012年11月6日 · Grb2-mediated regulation of FGFR basal phosphorylation opens a new window of opportunity for design of a novel class of modulators of FGF signaling. Specific inhibitors of dimeric Grb2 binding to FGFR could be used to promote FGF signaling in tissue repair and wound healing, whereas agents that augment Grb2-FGFR binding could find use for ...