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. ,
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