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Targeting of the Arf-like GTPase Arl3p to the Golgi requires N-terminal acetylation and the membrane protein Sys1p.

Nature cell biology | May 3, 2004

The GTPase Arl3p is required to recruit a second GTPase, Arl1p, to the Golgi in Saccharomyces cerevisiae. Arl1p binds to the GRIP domain, which is present in a number of long coiled-coil proteins or 'golgins'. Here we show that Arl3p is not myristoylated like most members of the Arf family, but is instead amino-terminally acetylated by the NatC complex. Targeting of Arl3p also requires a Golgi membrane protein Sys1p. The human homologues of Arl3p (Arf-related protein 1 (ARFRP1)) and Sys1p (hSys1) can be isolated in a complex after chemical cross-linking. This suggests that the targeting of ARFRP1/Arl3p to the Golgi is mediated by a direct interaction between its acetylated N terminus and Sys1p/hSys1.

Pubmed ID: 15077113 RIS Download

Mesh terms: ADP-Ribosylation Factor 1 | ADP-Ribosylation Factors | Acetylation | Acetyltransferases | Amino Acid Sequence | Animals | Arylamine N-Acetyltransferase | Carrier Proteins | Endoplasmic Reticulum | Golgi Apparatus | Humans | Macromolecular Substances | Membrane Proteins | Molecular Sequence Data | Monomeric GTP-Binding Proteins | Protein Structure, Tertiary | Protein Transport | Recombinant Fusion Proteins | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins | Sequence Alignment | Vesicular Transport Proteins

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