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The small GTPases Rab5a, Rab5b and Rab5c are differentially phosphorylated in vitro
Author(s) -
Chiariello Mario,
Bruni Carmelo B,
Bucci Cecilia
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00686-9
Subject(s) - rab , phosphorylation , gtpase , microbiology and biotechnology , kinase , biology , gene isoform , endocytosis , extracellular , map2k7 , biochemistry , cyclin dependent kinase 2 , protein kinase a , gene , receptor
Rab GTPases play a fundamental role in the regulation of membrane traffic. Three different Rab5 isoforms have been reported but no differences in their function in endocytosis have been discovered. As the Rab5 isoforms show a conserved consensus site for Ser/Thr phosphorylation, we investigated whether this site was phosphorylated. Here, we report that the three Rab5 proteins are differentially recognized by different kinases. Rab5a is efficiently phosphorylated by extracellular‐regulated kinase 1 but not by extracellular‐regulated kinase 2, while cdc2 kinase preferentially phosphorylates Ser‐123 of Rab5b. These findings strongly suggest that phosphorylation could be important to differentially regulate the function of the Rab5 isoforms.