Isoprenylation of Rab proteins possessing a C-terminal CaaX motif.
Rab proteins are small GTPases highly related to the yeast Ypt1 and Sec4 proteins involved in secretion. The Rab proteins were found associated with membranes of different compartments along the secretory and endocytic pathways. They share distinct C-terminal cysteine motifs required for membrane association. Unlike the other Rab proteins, Rab8, Rab11 and Rab13 terminate with a C-terminal CaaX motif similar to those of Ras/Rho proteins. This report demonstrates that Rab8 and Rab13 proteins are isoprenylated in vivo and geranylgeranylated in vitro. Rab11 associates in vitro geranylgeranylpyrophosphate and farnesylpyrophosphate. Our study shows that the CaaX motif is required for isoprenylation.
Joberty
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G
INSERM U248, Faculté de médecine Lariboisière Saint Louis, Paris, France.
Tavitian
A
A
Zahraoui
A
A
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D004247:DNA; D020558:GTP Phosphohydrolases / Q000737:chemistry / Q000378:metabolism*; D019204:GTP-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D017368:Protein Prenylation; D011994:Recombinant Proteins / Q000378:metabolism; D016415:Sequence Alignment; D020691:rab GTP-Binding Proteins
D011994:Recombinant Proteins; D004247:DNA; D020558:GTP Phosphohydrolases; D019204:GTP-Binding Proteins; C082377:RAB8A protein, human; D020691:rab GTP-Binding Proteins