Please use this identifier to cite or link to this item:
|Title:||G-Protein Binding features and regulation of the RalGDS family member, RGL2.||Authors:||Ferro, ELISA MARIA PAOLA
T. H., Fischer
G. C., White
|Issue Date:||2008||Project:||None||Journal:||BIOCHEMICAL JOURNAL||Abstract:||
RGL2 [RalGDS (Ral guanine nucleotide dissociation stimulator)-like 2] is a member of the RalGDS family that we have previouslyisolated and characterized as a potential effector for Ras and theRas analogue Rap1b. The protein shares 89% sequence identitywith its mouse orthologue Rlf (RalGDS-like factor). In the presentstudy we further characterized the G-protein-binding features ofRGL2 and also demonstrated that RGL2 has guanine-nucleotideexchangeactivity toward the small GTPase RalA. We found thatRGL2/Rlf properties are well conserved between human andmouse species. Both RGL2 and Rlf have a putative PKA (proteinkinase A) phosphorylation site at theC-terminal of the domain thatregulates the interaction with small GTPases. We demonstratedthat RGL2 is phosphorylated by PKA and phosphorylationreduces the ability of RGL2 to bind H-Ras. As RGL2 and Rlfare unique in the RalGDS family in having a PKA site in the Rasbindingdomain, the results of the present study indicate thatRas may distinguish between the different RalGDS familymembers by their phosphorylation by PKA.
|Appears in Collections:||Publications|
Show full item record
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.