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- Title
Targeting of the Arf-like GTPase Arl3p to the Golgi requires N-terminal acetylation and the membrane protein Sys1p.
- Authors
Behnia, Rudy; Panic, Bojana; Whyte, James R. C.; Munro, Sean
- Abstract
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.
- Subjects
GUANOSINE triphosphatase; PHOSPHATASES; GOLGI apparatus; MEMBRANE proteins; ACETYLATION; ORGANELLES
- Publication
Nature Cell Biology, 2004, Vol 6, Issue 5, p405
- ISSN
1465-7392
- Publication type
Article
- DOI
10.1038/ncb1120