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In addition to accelerate GTP gamma S binding by ARFs of all three classes, it appears to function preferentially as a guanine nucleotide exchange protein for ARF6, mediating internalisation of beta-1 integrin.. De plus, nous expédions IQSEC1 Anticorps (10) et beaucoup plus de produits pour cette protéine.
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both Arf6 (Montrer ARF6 Protéines) activation through GluN2B (Montrer GRIN2B Protéines)-BRAG1 during early development and the transition from BRAG1- to BRAG2-dependent Arf6 (Montrer ARF6 Protéines) signaling induced by the GluN2 subunit switch are critical for the development of mature glutamatergic synapses.
Brag2 is essential for developmental and pathological angiogenesis by promoting endothelial cell sprouting through regulation of adhesion by beta1-integrin internalization and link for the first time the process of beta1-integrin endocytosis with angiogenesis.
The EGFR (Montrer EGFR Protéines)-GEP100-Arf6 (Montrer ARF6 Protéines) axis affected the prognosis of patients with primary lung adenocarcinoma.
Data show that co-overexpression of GEP100 and AMAP1 (ASAP1 (Montrer ASAP1 Protéines)) correlates with rapidity of the local recurrence.
GEP100 regulates an Arf6 (Montrer ARF6 Protéines)/ERK (Montrer EPHB2 Protéines)/uPAR (Montrer PLAUR Protéines) signaling cascade in EGF (Montrer EGF Protéines)-induced breast cancer cell invasion.
GEP100 plays a significant role in pancreatic cancer invasion through regulating the expression of E-cadherin (Montrer CDH1 Protéines) and the process of mesenchymal to epithelial transition (MET).
BRAG2 acts at clathrin-coated pits to promote integrin internalization by activating Arf5 and suggest a previously unrecognized role for Arf5 in clathrin-mediated endocytosis of specific cargoes.
GEP100/Arf6 is required for epidermal growth factor-induced ERK/Rac1 signaling and cell migration in human hepatoma HepG2 cells.
The PH domain and the interdomain linker of Brag2 may be targets for selectively regulating the activity of Brag2.
Data suggest that GEP100-Arf6 (Montrer ARF6 Protéines)-AMAP1 (Montrer ASAP1 Protéines)-cortactin (Montrer CTTN Protéines) pathway, activated by VEGFR2 (Montrer KDR Protéines), appears to be common in angiogenesis and cancer invasion and metastasis, and provides their new therapeutic targets.
The present study provided evidence that BRAG2a is a novel component of the photoreceptor dystrophin (Montrer DMD Protéines)-associated glycoprotein complex (DGC (Montrer GGCX Protéines)), suggesting functional involvement of the BRAG2a-Arf6 (Montrer ARF6 Protéines) pathway downstream of the DGC (Montrer GGCX Protéines).
BRAG2 localized to postsynaptic processes at bipolar dyads, while BRAG3 localized to postsynaptic components at conventional synapses in mouse retina
In addition to accelerate GTP gamma S binding by ARFs of all three classes, it appears to function preferentially as a guanine nucleotide exchange protein for ARF6, mediating internalisation of beta-1 integrin.
ADP-ribosylation factors guanine nucleotide-exchange protein 100
, ADP-ribosylation factors guanine nucleotide-exchange protein 2
, IQ motif and SEC7 domain-containing protein 1
, brefeldin A-resistant ARF-GEF2
, brefeldin-resistant Arf-GEF 2 protein