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Published 25 October 2004. doi:10.1083/jcb.200407088
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 167, Number 2, 281-292
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Article

 The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to recruit the golgin Rud3p to the cis-Golgi

Alison K. Gillingham1, Amy Hin Yan Tong2,3, Charles Boone2,3, and Sean Munro1

1 Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 2QH, England, UK
2 Banting and Best Department of Medical Research, University of Toronto, Toronto ON, Canada M5G 1L6
3 Department of Medical Genetics and Microbiology, University of Toronto, Toronto ON, Canada M5G 1L6

Correspondence to Sean Munro: sean{at}mrc-lmb.cam.ac.uk

Rud3p is a coiled-coil protein of the yeast cis-Golgi. We find that Rud3p is localized to the Golgi via a COOH-terminal domain that is distantly related to the GRIP domain that recruits several coiled-coil proteins to the trans-Golgi by binding the small Arf-like GTPase Arl1p. In contrast, Rud3p binds to the GTPase Arf1p via this COOH-terminal "GRIP-related Arf-binding" (GRAB) domain. Deletion of RUD3 is lethal in the absence of the Golgi GTPase Ypt6p, and a screen of other mutants showing a similar genetic interaction revealed that Golgi targeting of Rud3p also requires Erv14p, a cargo receptor that cycles between the endoplasmic reticulum and Golgi. The one human protein with a GRAB domain, GMAP-210 (CEV14/Trip11/Trip230), is known to be on the cis-Golgi, but the COOH-terminal region that contains the GRAB domain has been reported to bind to centrosomes and {gamma}-tubulin (Rios, R.M, A. Sanchis, A.M. Tassin, C. Fedriani, and M. Bornens. 2004. Cell. 118:323–335). In contrast, we find that this region binds to the Golgi in a GRAB domain–dependent manner, suggesting that GMAP-210 may not link the Golgi to {gamma}-tubulin and centrosomes.

Abbreviations used in this paper: GA1, GRAB-associated 1; GRAB, GRIP-related Arf-binding.


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