Article abstract


Nature Cell Biology 6, 405 - 413 (2004)
Published online: 11 April 2004 | doi:10.1038/ncb1120

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

Rudy Behnia1,2, Bojana Panic1,2, James R. C. Whyte1 & Sean Munro1


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.

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  1. MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
  2. These authors contributed equally to this work.

Correspondence to: Sean Munro1 e-mail: sean@mrc-lmb.cam.ac.uk



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