Localization of ribophorin II to the endoplasmic reticulum involves both its transmembrane and cytoplasmic domains
Identifieur interne : 000671 ( Istex/Curation ); précédent : 000670; suivant : 000672Localization of ribophorin II to the endoplasmic reticulum involves both its transmembrane and cytoplasmic domains
Auteurs : Jie Fu ; Gregorio Pirozzi [États-Unis] ; Archana Sanjay [États-Unis] ; Robert Levy ; Yanru Chen ; Carmen De Lemos-Chiarandini ; David Sabatini ; Gert Kreibich [États-Unis]Source :
- European Journal of Cell Biology [ 0171-9335 ] ; 2000.
English descriptors
- Teeft :
- Adesnik, Amino, Amino acids, Biol, Blobel, Cdna, Cell biol, Cell biology, Cell surface, Chaperone, Chase period, Chimera, Chimeric, Cosson, Cytoplasmic, Cytoplasmic domain, Cytoplasmic domains, Dad1, Digestion, Distal regions, Domain, Ejcb, Embo, Endo, Endomembrane system, Endoplasmic, Endoplasmic reticulum, Final concentration, Golgi, Golgi apparatus, Hela cells, Immunofluorescence, Ivessa, Kreibich, Letourneur, Lipid bilayer, Localization, Localization signals, Luminal, Luminal domain, Luminal domains, Lysosomal, Lysosome, Machamer, Membrane, Membrane proteins, Methods enzymol, Microsome, Munro, Nilsson, Oligosaccharide, Oligosaccharyltransferase, Organelle, Permeabilized, Permeabilized cells, Pirozzi, Plasma membrane, Polypeptide, Receptor, Retention information, Retention signals, Reticulum, Retrieval, Retrieval signals, Ribophorin, Ribophorins, Ribosome, Ribosome binding, Rough endoplasmic reticulum, Rough microsomes, Sabatini, Short luminal, Subunit, Sugar residues, Transfected, Transfected cells, Translocation, Translocation apparatus, Transmembrane, Transmembrane domain, Transmembrane domains, Transmembrane proteins, Triton, York university.
Abstract
Summary Proteins that are concentrated in specific compartments of the endomembrane system in order to exert their organelle-specific function must possess specific localization signals that prevent their transport to distal regions of the exocytic pathway. Some resident proteins of the endoplasmic reticulum (ER) that are known to escape with low efficiency from this organelle to a post ER compartment are recognized by a recycling receptor and brought back to their site of residence. Other ER proteins, however, appear to be retained in the ER by mechanisms that operate in the organelle itself. The mammalian oligosaccharyltransferase (OST) is a protein complex that effects the cotranslational N-glycosylation of newly synthesized polypeptides, and is composed of at least four rough ER-specific membrane proteins: ribophorins I and II (RI and RII), OST48, and Dad1. The mechanism(s) by which the subunits of this complex are retained in the ER are not well understood. In an effort to identify the domains within RII responsible for its ER localization we have studied the fate of chimeric proteins in which one or more RII domains were replaced by the corresponding ones of the Tac antigen, the latter being a well characterized plasma membrane protein that lacks intrinsic ER retention signals and serves to provide a neutral framework for the identification of retention signals in other proteins. We found that the luminal domain of RII by itself does not contain retention information, while the cytoplasmic and transmembrane domains contain independent ER localization signals. We also show that the retention function of the transmembrane domain is strengthened by the presence of a flanking luminal region consisting of 15 amino acids.
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DOI: 10.1078/S0171-9335(04)70025-4
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Jie Fu<affiliation><mods:affiliation>Department of Cell Biology, New York University Medical Center, New YorkUSA</mods:affiliation><wicri:noCountry code="subField">YorkUSA</wicri:noCountry></affiliation><affiliation><mods:affiliation>Department of Cell Biology, New York University Medical Center, New YorkUSA</mods:affiliation><wicri:noCountry code="subField">YorkUSA</wicri:noCountry></affiliation><affiliation><mods:affiliation>Department of Cell Biology, New York University Medical Center, New YorkUSA</mods:affiliation><wicri:noCountry code="subField">YorkUSA</wicri:noCountry></affiliation><affiliation><mods:affiliation>Department of Cell Biology, New York University Medical Center, New YorkUSA</mods:affiliation><wicri:noCountry code="subField">YorkUSA</wicri:noCountry></affiliation><affiliation><mods:affiliation>Department of Cell Biology, New York University Medical Center, New YorkUSA</mods:affiliation><wicri:noCountry code="subField">YorkUSA</wicri:noCountry></affiliation>Le document en format XML
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first="Jie" last="Fu">Jie Fu</name><affiliation><mods:affiliation>Department of Cell Biology, New York University Medical Center, New YorkUSA</mods:affiliation><wicri:noCountry code="subField">YorkUSA</wicri:noCountry></affiliation></author><author><name sortKey="Pirozzi, Gregorio" sort="Pirozzi, Gregorio" uniqKey="Pirozzi G" first="Gregorio" last="Pirozzi">Gregorio Pirozzi</name><affiliation><mods:affiliation>Department of Cell Biology, New York University Medical Center, New YorkUSA</mods:affiliation></affiliation><affiliation wicri:level="2"><mods:affiliation>Present address: Axcell Biosciences, 201 College road East, Princeton, NJ 08540USA</mods:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">New Jersey</region></placeName><wicri:cityArea>Present address: Axcell Biosciences, 201 College road East, Princeton</wicri:cityArea></affiliation></author><author><name sortKey="Sanjay, Archana" sort="Sanjay, Archana" uniqKey="Sanjay A" first="Archana" last="Sanjay">Archana Sanjay</name><affiliation><mods:affiliation>Department of Cell Biology, New York University Medical Center, New YorkUSA</mods:affiliation></affiliation><affiliation wicri:level="2"><mods:affiliation>Present address: Department of Orthopaedics, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06510USA.</mods:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Connecticut</region></placeName><wicri:cityArea>Present address: Department of Orthopaedics, Yale University School of Medicine, 333 Cedar Street, New Haven</wicri:cityArea></affiliation></author><author><name sortKey="Levy, Robert" sort="Levy, Robert" uniqKey="Levy R" first="Robert" last="Levy">Robert Levy</name><affiliation><mods:affiliation>Department of Cell Biology, New York University Medical Center, New YorkUSA</mods:affiliation><wicri:noCountry code="subField">YorkUSA</wicri:noCountry></affiliation></author><author><name sortKey="Chen, Yanru" sort="Chen, Yanru" uniqKey="Chen Y" first="Yanru" last="Chen">Yanru Chen</name><affiliation><mods:affiliation>Department of Cell Biology, New York University Medical Center, New YorkUSA</mods:affiliation><wicri:noCountry code="subField">YorkUSA</wicri:noCountry></affiliation></author><author><name sortKey="De Lemos Chiarandini, Carmen" sort="De Lemos Chiarandini, Carmen" uniqKey="De Lemos Chiarandini C" first="Carmen" last="De Lemos-Chiarandini">Carmen De Lemos-Chiarandini</name><affiliation><mods:affiliation>Department of Cell Biology, New York University Medical Center, New YorkUSA</mods:affiliation><wicri:noCountry code="subField">YorkUSA</wicri:noCountry></affiliation></author><author><name sortKey="Sabatini, David" sort="Sabatini, David" uniqKey="Sabatini D" first="David" last="Sabatini">David Sabatini</name><affiliation><mods:affiliation>Department of Cell Biology, New York University Medical Center, New YorkUSA</mods:affiliation><wicri:noCountry code="subField">YorkUSA</wicri:noCountry></affiliation></author><author><name sortKey="Kreibich, Gert" sort="Kreibich, Gert" uniqKey="Kreibich G" first="Gert" last="Kreibich">Gert Kreibich</name><affiliation><mods:affiliation>Department of Cell Biology, New York University Medical Center, New YorkUSA</mods:affiliation></affiliation><affiliation><mods:affiliation>Dr. Gert Kreibich, Department of Cell Biology, New York University Medical Center, 550 First Avenue, New York, NY 10016USA, Fax: 2 12 2 63 81 39.</mods:affiliation></affiliation><affiliation wicri:level="1"><mods:affiliation>E-mail: kreibg01@mcrcr6.med.nyu.edu</mods:affiliation><country wicri:rule="url">États-Unis</country></affiliation></author></analytic><monogr></monogr><series><title level="j">European Journal of Cell Biology</title><title level="j" type="abbrev">EJCB</title><idno type="ISSN">0171-9335</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="2000">2000</date><biblScope unit="volume">79</biblScope><biblScope unit="issue">4</biblScope><biblScope unit="page" from="219">219</biblScope><biblScope unit="page" to="228">228</biblScope></imprint><idno type="ISSN">0171-9335</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0171-9335</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Adesnik</term><term>Amino</term><term>Amino acids</term><term>Biol</term><term>Blobel</term><term>Cdna</term><term>Cell biol</term><term>Cell biology</term><term>Cell surface</term><term>Chaperone</term><term>Chase period</term><term>Chimera</term><term>Chimeric</term><term>Cosson</term><term>Cytoplasmic</term><term>Cytoplasmic domain</term><term>Cytoplasmic domains</term><term>Dad1</term><term>Digestion</term><term>Distal regions</term><term>Domain</term><term>Ejcb</term><term>Embo</term><term>Endo</term><term>Endomembrane system</term><term>Endoplasmic</term><term>Endoplasmic reticulum</term><term>Final concentration</term><term>Golgi</term><term>Golgi apparatus</term><term>Hela cells</term><term>Immunofluorescence</term><term>Ivessa</term><term>Kreibich</term><term>Letourneur</term><term>Lipid bilayer</term><term>Localization</term><term>Localization signals</term><term>Luminal</term><term>Luminal domain</term><term>Luminal domains</term><term>Lysosomal</term><term>Lysosome</term><term>Machamer</term><term>Membrane</term><term>Membrane proteins</term><term>Methods enzymol</term><term>Microsome</term><term>Munro</term><term>Nilsson</term><term>Oligosaccharide</term><term>Oligosaccharyltransferase</term><term>Organelle</term><term>Permeabilized</term><term>Permeabilized cells</term><term>Pirozzi</term><term>Plasma membrane</term><term>Polypeptide</term><term>Receptor</term><term>Retention information</term><term>Retention signals</term><term>Reticulum</term><term>Retrieval</term><term>Retrieval signals</term><term>Ribophorin</term><term>Ribophorins</term><term>Ribosome</term><term>Ribosome binding</term><term>Rough endoplasmic reticulum</term><term>Rough microsomes</term><term>Sabatini</term><term>Short luminal</term><term>Subunit</term><term>Sugar residues</term><term>Transfected</term><term>Transfected cells</term><term>Translocation</term><term>Translocation apparatus</term><term>Transmembrane</term><term>Transmembrane domain</term><term>Transmembrane domains</term><term>Transmembrane proteins</term><term>Triton</term><term>York university</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract">Summary Proteins that are concentrated in specific compartments of the endomembrane system in order to exert their organelle-specific function must possess specific localization signals that prevent their transport to distal regions of the exocytic pathway. Some resident proteins of the endoplasmic reticulum (ER) that are known to escape with low efficiency from this organelle to a post ER compartment are recognized by a recycling receptor and brought back to their site of residence. Other ER proteins, however, appear to be retained in the ER by mechanisms that operate in the organelle itself. The mammalian oligosaccharyltransferase (OST) is a protein complex that effects the cotranslational N-glycosylation of newly synthesized polypeptides, and is composed of at least four rough ER-specific membrane proteins: ribophorins I and II (RI and RII), OST48, and Dad1. The mechanism(s) by which the subunits of this complex are retained in the ER are not well understood. In an effort to identify the domains within RII responsible for its ER localization we have studied the fate of chimeric proteins in which one or more RII domains were replaced by the corresponding ones of the Tac antigen, the latter being a well characterized plasma membrane protein that lacks intrinsic ER retention signals and serves to provide a neutral framework for the identification of retention signals in other proteins. We found that the luminal domain of RII by itself does not contain retention information, while the cytoplasmic and transmembrane domains contain independent ER localization signals. We also show that the retention function of the transmembrane domain is strengthened by the presence of a flanking luminal region consisting of 15 amino acids.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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