51. Golgi targeting of ARF-like GTPase Arl3p requires its Nalpha-acetylation and the integral membrane protein Sys1p.
- Author
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Setty SR, Strochlic TI, Tong AH, Boone C, and Burd CG
- Subjects
- ADP-Ribosylation Factors genetics, Acetylation, Arylamine N-Acetyltransferase genetics, Arylamine N-Acetyltransferase metabolism, N-Terminal Acetyltransferase B, Protein Transport physiology, Recombinant Fusion Proteins genetics, Recombinant Fusion Proteins metabolism, Saccharomyces cerevisiae genetics, Saccharomyces cerevisiae metabolism, Saccharomyces cerevisiae Proteins genetics, Vesicular Transport Proteins, ADP-Ribosylation Factors metabolism, Acetyltransferases metabolism, Golgi Apparatus metabolism, Membrane Proteins metabolism, Saccharomyces cerevisiae Proteins metabolism
- Abstract
Myristoylation of ARF family GTPases is required for their association with Golgi and endosomal membranes, where they regulate protein sorting and the lipid composition of these organelles. The Golgi-localized ARF-like GTPase Arl3p/ARP lacks a myristoylation signal, indicating that its targeting mechanism is distinct from myristoylated ARFs. We demonstrate that acetylation of the N-terminal methionine of Arl3p requires the NatC N(alpha)-acetyltransferase and that this modification is required for its Golgi localization. Chemical crosslinking and fluorescence microscopy experiments demonstrate that localization of Arl3p also requires Sys1p, a Golgi-localized integral membrane protein, which may serve as a receptor for acetylated Arl3p.
- Published
- 2004
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