Rer1p as common machinery for the endoplasmic reticulum localization of membrane proteins
Rer1p, a Golgi membrane protein, is required for the correct localization of an endoplasmic reticulum (ER) membrane protein, Sec12p, by a retrieval mechanism from the cis-Golgi to the ER. To test whether or not the role of Rer1p is common to multiple ER membrane proteins, we examined the localizatio...
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| Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 94; no. 18; pp. 9693 - 9698 |
|---|---|
| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
National Academy of Sciences of the United States of America
02.09.1997
National Acad Sciences National Academy of Sciences The National Academy of Sciences of the USA |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0027-8424 1091-6490 1091-6490 |
| DOI | 10.1073/pnas.94.18.9693 |
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| Abstract | Rer1p, a Golgi membrane protein, is required for the correct localization of an endoplasmic reticulum (ER) membrane protein, Sec12p, by a retrieval mechanism from the cis-Golgi to the ER. To test whether or not the role of Rer1p is common to multiple ER membrane proteins, we examined the localization of two other ER membrane proteins, Sec71p and Sec63p, in the wild-type and rer1 mutant yeast cells, using their fusions with an alpha-mating factor precursor (Mfalpha 1p). Although Sec71p and Sec63p have completely different topology from Sec12p, their Mfalpha 1p fusion proteins were also mislocalized to the trans-Golgi in the rer1 mutant. Overexpression of these fusions caused their mislocalization to the trans-Golgi even in the wild-type cells, and this mislocalization was partially suppressed by the co-overexpression of Rer1p. Either Sec71p or an artificial chimeric protein whose ER localization depends on Rer1p gave a competitive effect on the localization of the Mfalpha 1-Sec71p fusion, which was abolished in rer1. Thus, Rer1p appears to be one of the common limiting components in the retrieval machinery for ER membrane proteins. The results also suggest that Sec71p and Sec63p depend on ER-Golgi recycling, at least partly, for ER localization. We also examined the effect of a mutation in alpha-COP, a subunit of yeast coatomer, on the localization of these ER membrane proteins. The Mfalpha 1p fusions of Sec12p, Sec71p, and Sec63p were all more or less mislocalized in ret1-1. These observations imply that the roles of Rer1p an coatomer are much more general than thought before |
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| AbstractList | To test whether or not the role of Rer1p is common to multiple endoplasmic reticulum (ER) membrane proteins, Sato et al examined the localization of two other ER membrane proteins, Sec71p and Sec63p, in the wild-type and rer1 mutant yeast cells, using their fusions with an alpha-mating factor precursor. Rer1p, a Golgi membrane protein, is required for the correct localization of an endoplasmic reticulum (ER) membrane protein, Sec12p, by a retrieval mechanism from the cis-Golgi to the ER. To test whether or not the role of Rer1p is common to multiple ER membrane proteins, we examined the localization of two other ER membrane proteins, Sec71p and Sec63p, in the wild-type and rer1 mutant yeast cells, using their fusions with an α -mating factor precursor (Mfα 1p). Although Sec71p and Sec63p have completely different topology from Sec12p, their Mfα 1p fusion proteins were also mislocalized to the trans-Golgi in the rer1 mutant. Overexpression of these fusions caused their mislocalization to the trans-Golgi even in the wild-type cells, and this mislocalization was partially suppressed by the co-overexpression of Rer1p. Either Sec71p or an artificial chimeric protein whose ER localization depends on Rer1p gave a competitive effect on the localization of the Mfα 1p-Sec71p fusion, which was abolished in rer1. Thus, Rer1p appears to be one of the common limiting components in the retrieval machinery for ER membrane proteins. The results also suggest that Sec71p and Sec63p depend on ER-Golgi recycling, at least partly, for ER localization. We also examined the effect of a mutation in α -COP, a subunit of yeast coatomer, on the localization of these ER membrane proteins. The Mfα 1p fusions of Sec12p, Sec71p, and Sec63p were all more or less mislocalized in ret1-1. These observations imply that the roles of Rer1p and coatomer are much more general than thought before. Rer1p, a Golgi membrane protein, is required for the correct localization of an endoplasmic reticulum (ER) membrane protein, Sec12p, by a retrieval mechanism from the cis-Golgi to the ER. To test whether or not the role of Rer1p is common to multiple ER membrane proteins, we examined the localization of two other ER membrane proteins, Sec71p and Sec63p, in the wild-type and rer1 mutant yeast cells, using their fusions with an alpha-mating factor precursor (Mfalpha 1p). Although Sec71p and Sec63p have completely different topology from Sec12p, their Mfalpha 1p fusion proteins were also mislocalized to the trans-Golgi in the rer1 mutant. Overexpression of these fusions caused their mislocalization to the trans-Golgi even in the wild-type cells, and this mislocalization was partially suppressed by the co-overexpression of Rer1p. Either Sec71p or an artificial chimeric protein whose ER localization depends on Rer1p gave a competitive effect on the localization of the Mfalpha 1-Sec71p fusion, which was abolished in rer1. Thus, Rer1p appears to be one of the common limiting components in the retrieval machinery for ER membrane proteins. The results also suggest that Sec71p and Sec63p depend on ER-Golgi recycling, at least partly, for ER localization. We also examined the effect of a mutation in alpha-COP, a subunit of yeast coatomer, on the localization of these ER membrane proteins. The Mfalpha 1p fusions of Sec12p, Sec71p, and Sec63p were all more or less mislocalized in ret1-1. These observations imply that the roles of Rer1p an coatomer are much more general than thought before Rer1p, a Golgi membrane protein, is required for the correct localization of an endoplasmic reticulum (ER) membrane protein, Sec12p, by a retrieval mechanism from the cis-Golgi to the ER. To test whether or not the role of Rer1p is common to multiple ER membrane proteins, we examined the localization of two other ER membrane proteins, Sec71p and Sec63p, in the wild-type and rer1 mutant yeast cells, using their fusions with an alpha-mating factor precursor (Mfalpha1p). Although Sec71p and Sec63p have completely different topology from Sec12p, their Mfalpha1p fusion proteins were also mislocalized to the trans-Golgi in the rer1 mutant. Overexpression of these fusions caused their mislocalization to the trans-Golgi even in the wild-type cells, and this mislocalization was partially suppressed by the co-overexpression of Rer1p. Either Sec71p or an artificial chimeric protein whose ER localization depends on Rer1p gave a competitive effect on the localization of the Mfalpha1-Sec71p fusion, which was abolished in rer1. Thus, Rer1p appears to be one of the common limiting components in the retrieval machinery for ER membrane proteins. The results also suggest that Sec71p and Sec63p depend on ER-Golgi recycling, at least partly, for ER localization. We also examined the effect of a mutation in alpha-COP, a subunit of yeast coatomer, on the localization of these ER membrane proteins. The Mfalpha1p fusions of Sec12p, Sec71p, and Sec63p were all more or less mislocalized in ret1-1. These observations imply that the roles of Rer1p and coatomer are much more general than thought before.Rer1p, a Golgi membrane protein, is required for the correct localization of an endoplasmic reticulum (ER) membrane protein, Sec12p, by a retrieval mechanism from the cis-Golgi to the ER. To test whether or not the role of Rer1p is common to multiple ER membrane proteins, we examined the localization of two other ER membrane proteins, Sec71p and Sec63p, in the wild-type and rer1 mutant yeast cells, using their fusions with an alpha-mating factor precursor (Mfalpha1p). Although Sec71p and Sec63p have completely different topology from Sec12p, their Mfalpha1p fusion proteins were also mislocalized to the trans-Golgi in the rer1 mutant. Overexpression of these fusions caused their mislocalization to the trans-Golgi even in the wild-type cells, and this mislocalization was partially suppressed by the co-overexpression of Rer1p. Either Sec71p or an artificial chimeric protein whose ER localization depends on Rer1p gave a competitive effect on the localization of the Mfalpha1-Sec71p fusion, which was abolished in rer1. Thus, Rer1p appears to be one of the common limiting components in the retrieval machinery for ER membrane proteins. The results also suggest that Sec71p and Sec63p depend on ER-Golgi recycling, at least partly, for ER localization. We also examined the effect of a mutation in alpha-COP, a subunit of yeast coatomer, on the localization of these ER membrane proteins. The Mfalpha1p fusions of Sec12p, Sec71p, and Sec63p were all more or less mislocalized in ret1-1. These observations imply that the roles of Rer1p and coatomer are much more general than thought before. Rer1p, a Golgi membrane protein, is required for the correct localization of an endoplasmic reticulum (ER) membrane protein, Sec12p, by a retrieval mechanism from the cis-Golgi to the ER. To test whether or not the role of Rer1p is common to multiple ER membrane proteins, we examined the localization of two other ER membrane proteins, Sec71p and Sec63p, in the wild-type and rer1 mutant yeast cells, using their fusions with an alpha-mating factor precursor (Mfalpha 1p). Although Sec71p and Sec63p have completely different topology from Sec12p, their Mfalpha 1p fusion proteins were also mislocalized to the trans-Golgi in the rer1 mutant. Overexpression of these fusions caused their mislocalization to the trans-Golgi even in the wild-type cells, and this mislocalization was partially suppressed by the co-overexpression of Rer1p. Either Sec71p or an artificial chimeric protein whose ER localization depends on Rer1p gave a competitive effect on the localization of the Mfalpha 1-Sec71p fusion, which was abolished in rer1. Thus, Rer1p appears to be one of the common limiting components in the retrieval machinery for ER membrane proteins. The results also suggest that Sec71p and Sec63p depend on ER-Golgi recycling, at least partly, for ER localization. We also examined the effect of a mutation in alpha-COP, a subunit of yeast coatomer, on the localization of these ER membrane proteins. The Mfalpha 1p fusions of Sec12p, Sec71p, and Sec63p were all more or less mislocalized in ret1-1. These observations imply that the roles of Rer1p an coatomer are much more general than thought before. Rer1p, a Golgi membrane protein, is required for the correct localization of an endoplasmic reticulum (ER) membrane protein, Sec12p, by a retrieval mechanism from the cis -Golgi to the ER. To test whether or not the role of Rer1p is common to multiple ER membrane proteins, we examined the localization of two other ER membrane proteins, Sec71p and Sec63p, in the wild-type and rer1 mutant yeast cells, using their fusions with an α-mating factor precursor (Mfα1p). Although Sec71p and Sec63p have completely different topology from Sec12p, their Mfα1p fusion proteins were also mislocalized to the trans -Golgi in the rer1 mutant. Overexpression of these fusions caused their mislocalization to the trans -Golgi even in the wild-type cells, and this mislocalization was partially suppressed by the co-overexpression of Rer1p. Either Sec71p or an artificial chimeric protein whose ER localization depends on Rer1p gave a competitive effect on the localization of the Mfα1-Sec71p fusion, which was abolished in rer1 . Thus, Rer1p appears to be one of the common limiting components in the retrieval machinery for ER membrane proteins. The results also suggest that Sec71p and Sec63p depend on ER-Golgi recycling, at least partly, for ER localization. We also examined the effect of a mutation in α-COP, a subunit of yeast coatomer, on the localization of these ER membrane proteins. The Mfα1p fusions of Sec12p, Sec71p, and Sec63p were all more or less mislocalized in ret1–1 . These observations imply that the roles of Rer1p and coatomer are much more general than thought before. Rer1p, a Golgi membrane protein, is required for the correct localization of an endoplasmic reticulum (ER) membrane protein, Sec12p, by a retrieval mechanism from the cis -Golgi to the ER. To test whether or not the role of Rer1p is common to multiple ER membrane proteins, we examined the localization of two other ER membrane proteins, Sec71p and Sec63p, in the wild-type and rer1 mutant yeast cells, using their fusions with an α-mating factor precursor (Mfα1p). Although Sec71p and Sec63p have completely different topology from Sec12p, their Mfα1p fusion proteins were also mislocalized to the trans -Golgi in the rer1 mutant. Overexpression of these fusions caused their mislocalization to the trans -Golgi even in the wild-type cells, and this mislocalization was partially suppressed by the co-overexpression of Rer1p. Either Sec71p or an artificial chimeric protein whose ER localization depends on Rer1p gave a competitive effect on the localization of the Mfα1-Sec71p fusion, which was abolished in rer1 . Thus, Rer1p appears to be one of the common limiting components in the retrieval machinery for ER membrane proteins. The results also suggest that Sec71p and Sec63p depend on ER-Golgi recycling, at least partly, for ER localization. We also examined the effect of a mutation in α-COP, a subunit of yeast coatomer, on the localization of these ER membrane proteins. The Mfα1p fusions of Sec12p, Sec71p, and Sec63p were all more or less mislocalized in ret1–1 . These observations imply that the roles of Rer1p and coatomer are much more general than thought before. retrieval vesicle recycling Golgi apparatus coatomer Saccharomyces cerevisiae Rer1p, a Golgi membrane protein, is required for the correct localization of an endoplasmic reticulum (ER) membrane protein, Sec12p, by a retrieval mechanism from the cis-Golgi to the ER. To test whether or not the role of Rer1p is common to multiple ER membrane proteins, we examined the localization of two other ER membrane proteins, Sec71p and Sec63p, in the wild-type and rer1 mutant yeast cells, using their fusions with an alpha-mating factor precursor (Mfalpha1p). Although Sec71p and Sec63p have completely different topology from Sec12p, their Mfalpha1p fusion proteins were also mislocalized to the trans-Golgi in the rer1 mutant. Overexpression of these fusions caused their mislocalization to the trans-Golgi even in the wild-type cells, and this mislocalization was partially suppressed by the co-overexpression of Rer1p. Either Sec71p or an artificial chimeric protein whose ER localization depends on Rer1p gave a competitive effect on the localization of the Mfalpha1-Sec71p fusion, which was abolished in rer1. Thus, Rer1p appears to be one of the common limiting components in the retrieval machinery for ER membrane proteins. The results also suggest that Sec71p and Sec63p depend on ER-Golgi recycling, at least partly, for ER localization. We also examined the effect of a mutation in alpha-COP, a subunit of yeast coatomer, on the localization of these ER membrane proteins. The Mfalpha1p fusions of Sec12p, Sec71p, and Sec63p were all more or less mislocalized in ret1-1. These observations imply that the roles of Rer1p and coatomer are much more general than thought before. Rer1p, a Golgi membrane protein, is required for the correct localization of an endoplasmic reticulum (ER) membrane protein, Sec12p, by a retrieval mechanism from the cis-Golgi to the ER. To test whether or not the role of Rer1p is common to multiple ER membrane proteins, we examined the localization of two other ER membrane proteins, Sec71p and Sec63p, in the wild-type and rer1 mutant yeast cells, using their fusions with an α-mating factor precursor (Mfα1p). Although Sec71p and Sec63p have completely different topology from Sec12p, their Mfα1p fusion proteins were also mislocalized to the trans-Golgi in the rer1 mutant. Overexpression of these fusions caused their mislocalization to the trans-Golgi even in the wild-type cells, and this mislocalization was partially suppressed by the co-overexpression of Rer1p. Either Sec71p or an artificial chimeric protein whose ER localization depends on Rer1p gave a competitive effect on the localization of the Mfα1-Sec71p fusion, which was abolished in rer1. Thus, Rer1p appears to be one of the common limiting components in the retrieval machinery for ER membrane proteins. The results also suggest that Sec71p and Sec63p depend on ER-Golgi recycling, at least partly, for ER localization. We also examined the effect of a mutation in α-COP, a subunit of yeast coatomer, on the localization of these ER membrane proteins. The Mfα1p fusions of Sec12p, Sec71p, and Sec63p were all more or less mislocalized in ret1–1. These observations imply that the roles of Rer1p and coatomer are much more general than thought before. |
| Author | Sato, M Nakano, A Sato, K |
| AuthorAffiliation | Molecular Membrane Biology Laboratory, RIKEN (The Institute of Physical and Chemical Research), Wako, Saitama 351-01, Japan |
| AuthorAffiliation_xml | – name: Molecular Membrane Biology Laboratory, RIKEN (The Institute of Physical and Chemical Research), Wako, Saitama 351-01, Japan |
| Author_xml | – sequence: 1 fullname: Sato, K – sequence: 2 fullname: Sato, M – sequence: 3 fullname: Nakano, A |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/9275186$$D View this record in MEDLINE/PubMed |
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| Copyright | Copyright 1993-1997 National Academy of Sciences Copyright National Academy of Sciences Sep 2, 1997 Copyright © 1997, The National Academy of Sciences of the USA 1997 |
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| Notes | F60 1997061032 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 14 ObjectType-Article-1 ObjectType-Feature-2 content type line 23 To whom reprint requests should be addressed. Communicated by Randy Schekman, University of California, Berkeley, El Cerrito, CA |
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| Snippet | Rer1p, a Golgi membrane protein, is required for the correct localization of an endoplasmic reticulum (ER) membrane protein, Sec12p, by a retrieval mechanism... To test whether or not the role of Rer1p is common to multiple endoplasmic reticulum (ER) membrane proteins, Sato et al examined the localization of two other... |
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| SubjectTerms | Antibodies APARATO GOLGI APPAREIL DE GOLGI Biological Sciences CELL MEMBRANES Cellular biology DNA ENDOPLASMIC RETICULUM Endoplasmic Reticulum - metabolism Fungal Proteins Fungal Proteins - genetics Fungal Proteins - metabolism genetics GLICOPROTEINAS GLYCOPROTEINE GLYCOPROTEINS GOLGI APPARATUS IMMUNOCYTOCHEMISTRY IMMUNOLOGIE IMMUNOLOGY INMUNOLOGIA MEMBRANAS CELULARES MEMBRANE CELLULAIRE Membrane Proteins Membrane Proteins - genetics Membrane Proteins - metabolism Membranes metabolism METABOLISME DES PROTEINES METABOLISMO PROTEICO Overproduction Plasmids PROTEIN METABOLISM PROTEIN TRANSPORT PROTEINAS PROTEINE PROTEINS Receptors Recombinant Fusion Proteins Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism RETICULO ENDOPLASMATICO RETICULUM ENDOPLASMIQUE SACCHAROMYCES CEREVISIAE Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae - ultrastructure Saccharomyces cerevisiae Proteins Secretion ultrastructure Vesicular Transport Proteins Yeasts |
| Title | Rer1p as common machinery for the endoplasmic reticulum localization of membrane proteins |
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