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-nucleotideexchange 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 theC-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 Rasbinding domain, the results of the present study indicate that Ras may distinguish between the different RalGDS family members by their phosphorylation by PKA.

Ferro, E.M.P., D., M., P., G., T. H., F., S., P., Pogni, R., et al. (2008). G-Protein Binding features and regulation of the RalGDS family member, RGL2. BIOCHEMICAL JOURNAL, 415, 145-154 [10.1042/BJ20080255].

G-Protein Binding features and regulation of the RalGDS family member, RGL2.

FERRO, ELISA MARIA PAOLA;POGNI, REBECCA;TRABALZINI, LORENZA
2008-01-01

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-nucleotideexchange 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 theC-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 Rasbinding domain, the results of the present study indicate that Ras may distinguish between the different RalGDS family members by their phosphorylation by PKA.
Ferro, E.M.P., D., M., P., G., T. H., F., S., P., Pogni, R., et al. (2008). G-Protein Binding features and regulation of the RalGDS family member, RGL2. BIOCHEMICAL JOURNAL, 415, 145-154 [10.1042/BJ20080255].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11365/21698
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