Human ARHGEF2 ELISA Kit (V2LY-0626-LY3706)

Rho/Rac Guanine Nucleotide Exchange Factor 2

Activates Rho-GTPases by promoting the exchange of GDP for GTP. May be involved in epithelial barrier permeability, cell motility and polarization, dendritic spine morphology, antigen presentation, leukemic cell differentiation, cell cycle regulation, innate immune response, and cancer. Binds Rac-GTPases, but does not seem to promote nucleotide exchange activity toward Rac-GTPases, which was uniquely reported in PubMed:9857026. May stimulate instead the cortical activity of Rac. Inactive toward CDC42, TC10, or Ras-GTPases. Forms an intracellular sensing system along with NOD1 for the detection of microbial effectors during cell invasion by pathogens. Required for RHOA and RIP2 dependent NF-kappaB signaling pathways activation upon S.flexneri cell invasion. Involved not only in sensing peptidoglycan (PGN)-derived muropeptides through NOD1 that is independent of its GEF activity, but also in the activation of NF-kappaB by Shigella effector proteins (IpgB2 and OspB) which requires its GEF activity and the activation of RhoA. Involved in innate immune signaling transduction pathway promoting cytokine IL6/interleukin-6 and TNF-alpha secretion in macrophage upon stimulation by bacterial peptidoglycans; acts as a signaling intermediate between NOD2 receptor and RIPK2 kinase. Contributes to the tyrosine phosphorylation of RIPK2 through Src tyrosine kinase leading to NF-kappaB activation by NOD2. Overexpression activates Rho-, but not Rac-GTPases, and increases paracellular permeability (By similarity).
Involved in neuronal progenitor cell division and differentiation (PubMed:28453519).
Involved in the migration of precerebellar neurons (By similarity).

Actin filament organization Source: UniProtKB
Asymmetric neuroblast division Source: UniProtKB
Cell cycle Source: UniProtKB-KW
Cell morphogenesis Source: UniProtKB
Cellular hyperosmotic response Source: BHF-UCL
Cellular response to muramyl dipeptide Source: UniProtKB
Cellular response to tumor necrosis factor Source: BHF-UCL
G protein-coupled receptor signaling pathway Source: Reactome
Innate immune response Source: UniProtKB-KW
Intracellular protein transport Source: UniProtKB
Intracellular signal transduction Source: InterPro
Negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
Negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress Source: BHF-UCL
Negative regulation of microtubule depolymerization Source: UniProtKB
Negative regulation of necroptotic process Source: BHF-UCL
Positive regulation of apoptotic process Source: Reactome
Positive regulation of interleukin-6 production Source: UniProtKB
Positive regulation of neuron differentiation Source: UniProtKB
Positive regulation of neuron migration Source: UniProtKB
Positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
Positive regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
Positive regulation of transcription by RNA polymerase II Source: UniProtKB
Positive regulation of tumor necrosis factor production Source: UniProtKB
Regulation of cell population proliferation Source: UniProtKB
Regulation of Rho protein signal transduction Source: GO_Central
Regulation of small GTPase mediated signal transduction Source: Reactome

Ruffle membrane; Golgi apparatus; Cytoskeleton; Spindle; Cytoplasm; Tight junction; Cytoplasmic vesicle. Localizes to the tips of cortical microtubules of the mitotic spindle during cell division, and is further released upon microtubule depolymerization (PubMed:15827085). Recruited into membrane ruffles induced by S.flexneri at tight junctions of polarized epithelial cells (PubMed:19043560). Colocalized with NOD2 and RIPK2 in vesicles and with the cytoskeleton (PubMed:21887730).

Neurodevelopmental disorder with midbrain and hindbrain malformations (NEDMHM): An autosomal recessive neurodevelopmental disorder characterized by intellectual disability, speech delay, mild microcephaly, midbrain-hindbrain malformations, and variable dysmorphic features.

Phosphorylation of Ser-886 by PAK1 induces binding to protein YWHAZ, promoting its relocation to microtubules and the inhibition of its activity. Phosphorylated by AURKA and CDK1 during mitosis, which negatively regulates its activity. Phosphorylation by MAPK1 or MAPK3 increases nucleotide exchange activity. Phosphorylation by PAK4 releases GEF-H1 from the microtubules. Phosphorylated on serine, threonine and tyrosine residues in a RIPK2-dependent manner.