ARHGEF2

Rho guanine nucleotide exchange factor 2 ;
Guanine nucleotide exchange factor H1 ;
GEF-H1 ;
Microtubule-regulated Rho-GEF ;
Proliferating cell nucleolar antigen p40 ;

domain:The DH (DBL-homology) domain interacts with and promotes loading of GTP on RhoA.,domain:The PH (pleckstrin-homology) domain is involved in microtubule binding and targeting to tight junctions.,function: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, 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.,online information:ARHGEF2 entry,PTM:Phosphorylation of Ser-886 by PAK1 induces binding to protein 14-3-3 zeta, promoting its relocation to microtubules and the inhibition of its activity. Phosphorylated by STK6 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.,sequence caution:Sequence differs at a large extent from the sequence shown in the paper.,similarity:Contains 1 DH (DBL-homology) domain.,similarity:Contains 1 PH domain.,similarity:Contains 1 phorbol-ester/DAG-type zinc finger.,subcellular location:Localizes to the tips of cortical microtubules of the mitotic spindle during cell division, and is further released upon microtubule depolymerization.,subunit:Interacts with 14-3-3 zeta; when phosphorylated at Ser-886. Interacts with the kinases PAK4, AURKA/STK6 and MAPK1. Interacts with RHOA and RAC1.,

M phase of mitotic cell cycle, mitotic cell cycle, M phase, nuclear division, cell morphogenesis, intracellular protein transport, apoptosis, induction of apoptosis, cytoskeleton organization, actin filament organization, negative regulation of microtubule depolymerization, cell cycle, mitosis, intracellular signaling cascade, protein localization, cell death, induction of apoptosis by extracellular signals, negative regulation of organelle organization, regulation of cell death, positive regulation of cell death, programmed cell death, induction of programmed cell death, protein transport,death, cell cycle process, cell cycle phase, actin filament-based process, actin cytoskeleton organization, regulation of microtubule polymerization or depolymerization, negative regulation of microtubule polymerization or depolymerization, regulation of microtubule depolymerization, regulation of microtubule-based process, cellular component morphogenesis, regulation of organelle organization, cellular protein localization, regulation of Rho protein signal transduction, regulation of cell proliferation, regulation of apoptosis, positive regulation of apoptosis, regulation of programmed cell death, positive regulation of programmed cell death, negative regulation of protein complex disassembly, regulation of protein complex disassembly, establishment of protein localization, regulation of Ras protein signal transduction, intracellular transport, organelle fission, regulation of small GTPase mediated signal transduction, negative regulation of cellular component organization, cell division, regulation of cytoskeleton organization, negative regulation of cytoskeleton organization, regulation of microtubule cytoskeleton organization,cellular macromolecule localization,

Cytoplasm, cytoskeleton . Cytoplasm . Cell junction, tight junction . Golgi apparatus . Cytoplasm, cytoskeleton, spindle . Cell projection, ruffle membrane . 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). .