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 γ-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 γ-tubulin and centrosomes.
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25 October 2004
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October 25 2004
The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to recruit the golgin Rud3p to the cis-Golgi
Alison K. Gillingham,
Alison K. Gillingham
1Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 2QH, England, UK
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Amy Hin Yan Tong,
Amy Hin Yan Tong
2Banting and Best Department of Medical Research, University of Toronto, Toronto ON, Canada M5G 1L6
3Department of Medical Genetics and Microbiology, University of Toronto, Toronto ON, Canada M5G 1L6
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Charles Boone,
Charles Boone
2Banting and Best Department of Medical Research, University of Toronto, Toronto ON, Canada M5G 1L6
3Department of Medical Genetics and Microbiology, University of Toronto, Toronto ON, Canada M5G 1L6
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Sean Munro
Sean Munro
1Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 2QH, England, UK
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Alison K. Gillingham
1Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 2QH, England, UK
Amy Hin Yan Tong
2Banting and Best Department of Medical Research, University of Toronto, Toronto ON, Canada M5G 1L6
3Department of Medical Genetics and Microbiology, University of Toronto, Toronto ON, Canada M5G 1L6
Charles Boone
2Banting and Best Department of Medical Research, University of Toronto, Toronto ON, Canada M5G 1L6
3Department of Medical Genetics and Microbiology, University of Toronto, Toronto ON, Canada M5G 1L6
Sean Munro
1Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 2QH, England, UK
Correspondence to Sean Munro: [email protected]
Abbreviations used in this paper: GA1, GRAB-associated 1; GRAB, GRIP-related Arf-binding.
Received:
July 14 2004
Accepted:
September 07 2004
Online ISSN: 1540-8140
Print ISSN: 0021-9525
The Rockefeller University Press
2004
J Cell Biol (2004) 167 (2): 281–292.
Article history
Received:
July 14 2004
Accepted:
September 07 2004
Citation
Alison K. Gillingham, Amy Hin Yan Tong, Charles Boone, Sean Munro; The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to recruit the golgin Rud3p to the cis-Golgi . J Cell Biol 25 October 2004; 167 (2): 281–292. doi: https://doi.org/10.1083/jcb.200407088
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