Article abstract
Nature Cell Biology 6, 414 - 419 (2004)
Published online: 11 April 2004 | Corrected online: 30 April 2004 | doi:10.1038/ncb1121
Golgi targeting of ARF-like GTPase Arl3p requires its N
-acetylation and the integral membrane protein Sys1p
Subba Rao Gangi Setty1, Todd I. Strochlic1, Amy Hin Yan Tong2, Charles Boone2 & Christopher G. Burd1
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
-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.
- Department of Cell and Developmental Biology, University of Pennsylvania School of Medicine, 421 Curie Blvd. BRB 2/3 room 1010, Philadelphia, PA 19104-6058, USA.
- Banting and Best Department of Medical Research, University of Toronto, Toronto ON, M5G 1L6, Canada.
Correspondence to: Christopher G. Burd1 e-mail: cburd@mail.med.upenn.edu
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