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The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to recruit the golgin Rud3p to the cis-Golgi
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 bin...
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2004
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172552/ https://www.ncbi.nlm.nih.gov/pubmed/15504911 http://dx.doi.org/10.1083/jcb.200407088 |
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author | Gillingham, Alison K. Tong, Amy Hin Yan Boone, Charles Munro, Sean |
author_facet | Gillingham, Alison K. Tong, Amy Hin Yan Boone, Charles Munro, Sean |
author_sort | Gillingham, Alison K. |
collection | PubMed |
description | 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. |
format | Text |
id | pubmed-2172552 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2004 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21725522008-03-05 The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to recruit the golgin Rud3p to the cis-Golgi Gillingham, Alison K. Tong, Amy Hin Yan Boone, Charles Munro, Sean J Cell Biol Research Articles 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. The Rockefeller University Press 2004-10-25 /pmc/articles/PMC2172552/ /pubmed/15504911 http://dx.doi.org/10.1083/jcb.200407088 Text en Copyright © 2004, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Research Articles Gillingham, Alison K. Tong, Amy Hin Yan Boone, Charles Munro, Sean The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to recruit the golgin Rud3p to the cis-Golgi |
title | The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to recruit the golgin Rud3p to the cis-Golgi |
title_full | The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to recruit the golgin Rud3p to the cis-Golgi |
title_fullStr | The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to recruit the golgin Rud3p to the cis-Golgi |
title_full_unstemmed | The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to recruit the golgin Rud3p to the cis-Golgi |
title_short | The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to recruit the golgin Rud3p to the cis-Golgi |
title_sort | gtpase arf1p and the er to golgi cargo receptor erv14p cooperate to recruit the golgin rud3p to the cis-golgi |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172552/ https://www.ncbi.nlm.nih.gov/pubmed/15504911 http://dx.doi.org/10.1083/jcb.200407088 |
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