Access
To read this article in full you may need to log in, make a payment or gain access through a site license (see right).
Article
Nature Cell Biology 6, 414–419 (1 May 2004) | doi:10.1038/ncb1121
Golgi targeting of ARF-like GTPase Arl3p requires its N|[alpha]|-acetylation and the integral membrane protein Sys1p
&
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 Nα-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.
To read this article in full you may need to log in, make a payment or gain access through a site license (see right).
