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Literature summary for 3.6.5.1 extracted from

  • van Unen, J.; Yin, T.; Wu, Y.I.; Mastop, M.; Gadella, T.W.; Goedhart, J.
    Kinetics of recruitment and allosteric activation of ARHGEF25 isoforms by the heterotrimeric G-protein Galphaq (2016), Sci. Rep., 6, 36825 .
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Homo sapiens 5829
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GTP + H2O Homo sapiens
-
GDP + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
HeLa cell
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + H2O
-
Homo sapiens GDP + phosphate
-
?

Synonyms

Synonyms Comment Organism
Galphaq
-
Homo sapiens
heterotrimeric G-protein
-
Homo sapiens

General Information

General Information Comment Organism
metabolism Rho guanine nucleotide exchange factor p63RhoGEF619 relocates to the plasma membrane upon activation of Galphaq coupled GPCRs, resembling the well-known activation mechanism of Rho guanine nucleotide exchange factors (RhoGEFs) activated by Galpha12/13. Synthetic recruitment of p63RhoGEF619 to the plasma membrane increases RhoGEF activity towards GTPase RhoA, but full activation requires allosteric activation via Galphaq, overview. Dual role for heterotrimeric G-protein Galphaq in RhoGEF activation, as it both recruits and allosterically activates cytosolic ARHGEF25 gene encoding three RhoGEF isoforms. Activation of the heterotrimeric G-protein Galphaq relieves the DH domain of p63RhoGEF from its autoinhibited state by allosteric interaction with the PH domain Homo sapiens