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G-protein binding features and regulation of the RalGDS family member, RGL2. Biochem J 2008 Oct 01;415(1):145-54

Date

06/11/2008

Pubmed ID

18540861

DOI

10.1042/BJ20080255

Abstract

RGL2 [RalGDS (Ral guanine nucleotide dissociation stimulator)-like 2] is a member of the RalGDS family that we have previously isolated and characterized as a potential effector for Ras and the Ras analogue Rap1b. The protein shares 89% sequence identity with its mouse orthologue Rlf (RalGDS-like factor). In the present study we further characterized the G-protein-binding features of RGL2 and also demonstrated that RGL2 has guanine-nucleotide-exchange activity toward the small GTPase RalA. We found that RGL2/Rlf properties are well conserved between human and mouse species. Both RGL2 and Rlf have a putative PKA (protein kinase A) phosphorylation site at the C-terminal of the domain that regulates the interaction with small GTPases. We demonstrated that RGL2 is phosphorylated by PKA and phosphorylation reduces the ability of RGL2 to bind H-Ras. As RGL2 and Rlf are unique in the RalGDS family in having a PKA site in the Ras-binding domain, the results of the present study indicate that Ras may distinguish between the different RalGDS family members by their phosphorylation by PKA.

Author List

Ferro E, Magrini D, Guazzi P, Fischer TH, Pistolesi S, Pogni R, White GC, Trabalzini L

Author

Gilbert C. White MD Professor in the Medicine department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Amino Acid Sequence
Animals
Cells, Cultured
Cyclic AMP-Dependent Protein Kinases
Gene Deletion
Guanine Nucleotide Exchange Factors
Humans
Mice
Models, Molecular
Molecular Sequence Data
Monomeric GTP-Binding Proteins
Phosphorylation
Protein Structure, Tertiary
Recombinant Fusion Proteins
Sequence Alignment
Structure-Activity Relationship
Transcription Factors
Two-Hybrid System Techniques
rab GTP-Binding Proteins
ras Proteins
jenkins-FCD Prod-482 91ad8a360b6da540234915ea01ff80e38bfdb40a