Isoprenylation of rab proteins on structurally distinct cysteine motifs.

摘要: rab proteins are low molecular weight GTP-binding highly related to Ypt1p and Sec4p, which involved in the control of secretion yeast Saccharomyces cerevisiae. Morphological biochemical studies have shown that membrane associated localized specific subcompartments along exocytic endocytic pathway. Membrane association requires presence C-terminal cysteine residues. The present report indicates structurally distinct motifs subjected isoprenylation both vitro vivo. Studies on deletion mutants suggest an intact end is required for with necessary post-translational modification. Finally, we show isoprenoid transferase modifies termini different from enzyme farnesylates nuclear lamins ras vitro.