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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 (show CDK5 Proteins)-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 (show F11R Proteins) regulates epithelial permeability via association with ZO-2 (show TJP2 Proteins), afadin, and PDZ-GEF1 to activate Rap2c (show RAP2C Proteins) and control contraction of the apical cytoskeleton.
NEDD4-1 (show NEDD4 Proteins) 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 (show RABGEF1 Proteins)-ERK (show EPHB2 Proteins) signaling.
DNA methylation (show HELLS Proteins) shows genome-wide association of NFIX (show MLZE Proteins), RAPGEF2 and MSRB3 (show MSRB3 Proteins) 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
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 (show ADCY10 Proteins) 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 (show TERF2IP Proteins) signaling may lead to defective vascular morphogenesis in the yolk sac (show ADCY10 Proteins) 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