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.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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ADP-Ribosylation Factors / genetics
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ADP-Ribosylation Factors / metabolism*
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Acetylation
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Acetyltransferases / metabolism*
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Arylamine N-Acetyltransferase / genetics
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Arylamine N-Acetyltransferase / metabolism
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Golgi Apparatus / metabolism*
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Membrane Proteins / metabolism*
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N-Terminal Acetyltransferase B
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Protein Transport / physiology
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / metabolism
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism*
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Vesicular Transport Proteins
Substances
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MAK10 protein, S cerevisiae
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Membrane Proteins
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Recombinant Fusion Proteins
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Saccharomyces cerevisiae Proteins
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Sys1 protein, S cerevisiae
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Vesicular Transport Proteins
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Acetyltransferases
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N-Terminal Acetyltransferase B
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MAK3 protein, S cerevisiae
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Arylamine N-Acetyltransferase
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ADP-Ribosylation Factors
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ARL3 protein, S cerevisiae