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anti-Human RAPGEF2 Antikörper:
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Human Polyclonal RAPGEF2 Primary Antibody für ICC, IF - ABIN438495
Emery, Eiden, Mustafa, Eiden: Rapgef2 connects GPCR-mediated cAMP signals to ERK activation in neuronal and endocrine cells. in Science signaling 2013
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Human Monoclonal RAPGEF2 Primary Antibody für ELISA, WB - ABIN564181
Letschka, Kollmann, Pfeifhofer-Obermair, Lutz-Nicoladoni, Obermair, Fresser, Leitges, Hermann-Kleiter, Kaminski, Baier: PKC-theta selectively controls the adhesion-stimulating molecule Rap1. in Blood 2008
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Bat Polyclonal RAPGEF2 Primary Antibody für WB - ABIN6746202
Blake, Nawrotzki, Peters, Froehner, Davies: Isoform diversity of dystrobrevin, the murine 87-kDa postsynaptic protein. in The Journal of biological chemistry 1996
We report that in response to factors that promote cell motility, the Rap guanine exchange factor RAPGEF2 is rapidly phosphorylated by I-kappa-B-kinase-beta and casein kinase-1alpha and consequently degraded by the proteasome.
Data indicate that Rapgef2 is a cAMP-binding protein present in chromaffin cells.
Cdk5-mediated phosphorylation of RapGEF2 controls neuronal migration in the developing cerebral cortex.
local accumulation of PDZGEF at the apical membrane during establishment of epithelial polarity is mediated by electrostatic interactions between positively charged side chains in the PDZ domain and negatively charged phosphatidic acid.
SCF(FBXW11) bound, polyubiquitylated, and destabilized RAPGEF2, a guanine nucleotide exchange factor that activates the small GTPase RAP1
JAM-A regulates epithelial permeability via association with ZO-2, afadin, and PDZ-GEF1 to activate Rap2c and control contraction of the apical cytoskeleton.
NEDD4-1 regulates cell migration and invasion through ubiquitination of CNrasGEF in vitro.
Data indicate that expression of Rapgef2 in embryonic kidney 293T cells enables cAMP-Rap1-ERK signaling.
DNA methylation shows genome-wide association of NFIX, RAPGEF2 and MSRB3 with gestational age at birth.
PDZ-GEF activates Rap1 under resting conditions to stabilize cell-cell junctions and maintain basal integrity
Regulation of G protein-linked guanine nucleotide exchange factors for Rho, PDZ-RhoGEF, and LARG by tyrosine phosphorylation: evidence of a role for focal adhesion kinase
PSD-95/Dlg/ZO-1 homology (PDZ)-RhoGEF was isolated from mouse brain as a plexin-B1-specific interacting protein
Data show that the interaction of PDZ-GEF1 with an internalized neurotrophin receptor transported to late endosomes induces sustained activation of both Rap1 and ERK and neurite outgrowth.
Rapgef2-conditional knockout (cKO) mice and Rapgef6-KO mice exhibited hyperlocomotion phenotype and working-memory defect, both of which could be recognized as schizophrenia-like behavior.
This study showed here that the guanine nucleotide exchange factor NCS-Rapgef2 is encoded by a neuron-specific transcript from the Rapgef2 gene locus, and functions as an obligate cAMP sensor for dopamine-dependent ERK activation in hippocampus, amygdala, and ventral striatum
Study show that double knockout of Rapgef6 in Rapgef2-cKO mice (Rapgef2/6-dKO) results in marked enlargement of the ectopic cortical mass. While Rapgef2-cKO affects late-born neurons only, Rapgef2/6-dKO affects both early-born and late-born neurons in the developing brain.
These results indicate a crucial role of the Rapgef2-Rap1A-ERK-c-jun pathway in regulation of the AJ formation in RGCs.
The essential role of RA-GEF-1 is the proper formation of the cerebral midline commissures.
Rapgef2 deficiency led to embryonic lethality at E11.5 due to severe yolk sac vascular defects.
Our findings suggest a crucial function of RA-GEF-1 in neural migration
CNrasGEF regulates melanogenesis but that it also has a distinct role in regulating cell proliferation/apoptosis
These results suggest that deficient Rap1 signaling may lead to defective vascular morphogenesis in the yolk sac and embryos proper.
the role of RA-GEF-1 in embryonic vascular network formation was investigated.
Members of the RAS (see HRAS\; MIM 190020) subfamily of GTPases function in signal transduction as GTP/GDP-regulated switches that cycle between inactive GDP- and active GTP-bound states. Guanine nucleotide exchange factors (GEFs), such as RAPGEF2, serve as RAS activators by promoting acquisition of GTP to maintain the active GTP-bound state and are the key link between cell surface receptors and RAS activation (Rebhun et al., 2000
Rap guanine nucleotide exchange factor (GEF) 2
, rap guanine nucleotide exchange factor 2
, Rap guanine nucleotide exchange factor 2-like
, rap guanine nucleotide exchange factor 2-like
, PDZ domain containing guanine nucleotide exchange factor (GEF) 1
, PDZ domain-containing guanine nucleotide exchange factor 1
, neural RAP guanine nucleotide exchange protein