Identifiers
RhoA_GEFs*
Rho guanine nucleotide exchange factor (GEF) 1
HUGO:ARHGEF1, HGNC:681, ENTREZ:9138, GENECARDS:GC19P042387, UNIPROT:Q92888
Rho/Rac guanine nucleotide exchange factor (GEF) 2
HUGO:ARHGEF2, HGNC:682, ENTREZ:9181, GENECARDS:GC01M155916, UNIPROT:Q92974
Rho guanine nucleotide exchange factor (GEF) 3
HUGO:ARHGEF3, HGNC:683, ENTREZ:50650, GENECARDS:GC03M056736, UNIPROT:Q9NR81
Rho guanine nucleotide exchange factor (GEF) 4
HUGO:ARHGEF4, HGNC:684, ENTREZ:50649, GENECARDS:GC02P131595, UNIPROT:Q9NR80
Rho guanine nucleotide exchange factor (GEF) 10-like
HUGO:ARHGEF10L, HGNC:25540, ENTREZ:55160, GENECARDS:GC01P017866, UNIPROT:Q9HCE6
Rho guanine nucleotide exchange factor (GEF) 12
HUGO:ARHGEF12, HGNC:14193, ENTREZ:23365, GENECARDS:GC11P120207, UNIPROT:Q9NZN5
MCF.2 cell line derived transforming sequence-like
HUGO:MCF2L, HGNC:14576, ENTREZ:23263, GENECARDS:GC13P113548, UNIPROT:O15068
neuronal guanine nucleotide exchange factor
HUGO:NGEF, HGNC:7807, ENTREZ:25791 , GENECARDS:GC02M233707 , UNIPROT:Q8N5V2
epithelial cell transforming sequence 2 oncogene
HUGO:ECT2, HGNC:3155, ENTREZ:1894, GENECARDS:GC03P172468, UNIPROT:Q9H8V3
RAP1, GTP-GDP dissociation stimulator 1
HUGO:RAP1GDS1, HGNC:9859, ENTREZ:5910, GENECARDS:GC04P099182, UNIPROT:P52306
vav 2 guanine nucleotide exchange factor
HUGO:VAV2, HGNC:12658, ENTREZ:7410, GENECARDS:GC09M136627, UNIPROT:P52735
Maps_Modules
HMC:ACTIVATING_INVASION_AND_METASTASIS
EMT Senescence / EMT_REGULATORS
EMT Senescence / CYTOSKELETON_POLARITY
References
PMID:9789025
PMID:9641915
p115RhoGEF(so-called ARHGEF1) is an Rho guanine nucleotide exchange factor.
References
em_emtc_emtc_re693( EMT Senescence ):
PMID:11149925
2 classes of negative regulators of Rho proteins have been described. GAPs and GDIs.
Rho proteins have relatively slow intrinsic rates of GTP hydrolysis that can be accelerated by GAPs (GTPase activating proteins).
Another class of proteins shown to inhibit the release of GDP from Rho proteins, GDIs (GDP Dissociation Inhibitors (GDIs) have been described.
Perhaps more important than their effects on the GDP/GTP cycle is the ability of GDIs to solubilize membrane-associated Rho proteins.
RhoA is sequestered in the cytosol by a RhoGDI-dependent and -independent mechanisms.
RhoGDI binding is not affected by the length of the prenyl chain (farnesylation versus geranylgeranylation)
Palmitoylation blocks RhoGDI binding.
PMID:9113980
GDIs play a primary role in modulating the activation of GTPases and may also be critical for the cellular compartmentalization of GTPases.
em_emtc_emtc_re734( EMT Senescence ):
PMID:16112081
In vitro, GrinchGEF (ARHGEF10L) induced the GDP/ GTP exchange at RhoA, but not at Rac1 or Cdc42.
In intact cells, GrinchGEF induced specifically Rho activation and enhanced RhoA,B,C-specific downstream effect.
GrinchGEF, similar to its relative p164-RhoGEF (ARHGEF17), is a Rho-specific GEF.
Although RhoA, B, and C have different cellular functions, and some regulators and effectors show preferential interaction with these Rho isoforms, GrinchGEF apparently does not distinguish between RhoA,B,C and similarly activates these Rho proteins
em_emtc_emtc_re735( EMT Senescence ):
PMID:9822605
Phosphorylated Vav-2 was found to be active on RhoA, RhoB and the more distantly related RhoG protein