Rsp5 Ubiquitin Ligase Is Required for Protein Trafficking in Saccharomyces cerevisiae COPI Mutants

Retrograde trafficking from the Golgi to the endoplasmic reticulum (ER) depends on the formation of vesicles coated with the multiprotein complex COPI. In Saccharomyces cerevisiae ubiquitinated derivatives of several COPI subunits have been identified. The importance of this modification of COPI pro...

Full description

Bibliographic Details
Main Authors:	Jarmoszewicz, Katarzyna, Łukasiak, Katarzyna, Riezman, Howard, Kaminska, Joanna
Format:	Online
Language:	English
Published:	Public Library of Science 2012
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3383674/

id	pubmed-3383674
recordtype	oai_dc
spelling	pubmed-33836742012-07-03 Rsp5 Ubiquitin Ligase Is Required for Protein Trafficking in Saccharomyces cerevisiae COPI Mutants Jarmoszewicz, Katarzyna Łukasiak, Katarzyna Riezman, Howard Kaminska, Joanna Research Article Retrograde trafficking from the Golgi to the endoplasmic reticulum (ER) depends on the formation of vesicles coated with the multiprotein complex COPI. In Saccharomyces cerevisiae ubiquitinated derivatives of several COPI subunits have been identified. The importance of this modification of COPI proteins is unknown. With the exception of the Sec27 protein (β’COP) neither the ubiquitin ligase responsible for ubiquitination of COPI subunits nor the importance of this modification are known. Here we find that the ubiquitin ligase mutation, rsp5-1, has a negative effect that is additive with ret1-1 and sec28Δ mutations, in genes encoding α- and ε-COP, respectively. The double ret1-1 rsp5-1 mutant is also more severely defective in the Golgi-to-ER trafficking compared to the single ret1-1, secreting more of the ER chaperone Kar2p, localizing Rer1p mostly to the vacuole, and increasing sensitivity to neomycin. Overexpression of ubiquitin in ret1-1 rsp5-1 mutant suppresses vacuolar accumulation of Rer1p. We found that the effect of rsp5 mutation on the Golgi-to-ER trafficking is similar to that of sla1Δ mutation in a gene encoding actin cytoskeleton proteins, an Rsp5p substrate. Additionally, Rsp5 and Sla1 proteins were found by co-immunoprecipitation in a complex containing COPI subunits. Together, our results show that Rsp5 ligase plays a role in regulating retrograde Golgi-to-ER trafficking. Public Library of Science 2012-06-26 /pmc/articles/PMC3383674/ /pubmed/22761830 http://dx.doi.org/10.1371/journal.pone.0039582 Text en Jarmoszewicz et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Jarmoszewicz, Katarzyna Łukasiak, Katarzyna Riezman, Howard Kaminska, Joanna
spellingShingle	Jarmoszewicz, Katarzyna Łukasiak, Katarzyna Riezman, Howard Kaminska, Joanna Rsp5 Ubiquitin Ligase Is Required for Protein Trafficking in Saccharomyces cerevisiae COPI Mutants
author_facet	Jarmoszewicz, Katarzyna Łukasiak, Katarzyna Riezman, Howard Kaminska, Joanna
author_sort	Jarmoszewicz, Katarzyna
title	Rsp5 Ubiquitin Ligase Is Required for Protein Trafficking in Saccharomyces cerevisiae COPI Mutants
title_short	Rsp5 Ubiquitin Ligase Is Required for Protein Trafficking in Saccharomyces cerevisiae COPI Mutants
title_full	Rsp5 Ubiquitin Ligase Is Required for Protein Trafficking in Saccharomyces cerevisiae COPI Mutants
title_fullStr	Rsp5 Ubiquitin Ligase Is Required for Protein Trafficking in Saccharomyces cerevisiae COPI Mutants
title_full_unstemmed	Rsp5 Ubiquitin Ligase Is Required for Protein Trafficking in Saccharomyces cerevisiae COPI Mutants
title_sort	rsp5 ubiquitin ligase is required for protein trafficking in saccharomyces cerevisiae copi mutants
description	Retrograde trafficking from the Golgi to the endoplasmic reticulum (ER) depends on the formation of vesicles coated with the multiprotein complex COPI. In Saccharomyces cerevisiae ubiquitinated derivatives of several COPI subunits have been identified. The importance of this modification of COPI proteins is unknown. With the exception of the Sec27 protein (β’COP) neither the ubiquitin ligase responsible for ubiquitination of COPI subunits nor the importance of this modification are known. Here we find that the ubiquitin ligase mutation, rsp5-1, has a negative effect that is additive with ret1-1 and sec28Δ mutations, in genes encoding α- and ε-COP, respectively. The double ret1-1 rsp5-1 mutant is also more severely defective in the Golgi-to-ER trafficking compared to the single ret1-1, secreting more of the ER chaperone Kar2p, localizing Rer1p mostly to the vacuole, and increasing sensitivity to neomycin. Overexpression of ubiquitin in ret1-1 rsp5-1 mutant suppresses vacuolar accumulation of Rer1p. We found that the effect of rsp5 mutation on the Golgi-to-ER trafficking is similar to that of sla1Δ mutation in a gene encoding actin cytoskeleton proteins, an Rsp5p substrate. Additionally, Rsp5 and Sla1 proteins were found by co-immunoprecipitation in a complex containing COPI subunits. Together, our results show that Rsp5 ligase plays a role in regulating retrograde Golgi-to-ER trafficking.
publisher	Public Library of Science
publishDate	2012
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3383674/
_version_	1611539222399811584

Rsp5 Ubiquitin Ligase Is Required for Protein Trafficking in Saccharomyces cerevisiae COPI Mutants

Similar Items