A short sequence in the COOH-terminus makes an adenovirus membrane glycoprotein a resident of the endoplasmic reticulum
Identifieur interne : 000806 ( Istex/Corpus ); précédent : 000805; suivant : 000807A short sequence in the COOH-terminus makes an adenovirus membrane glycoprotein a resident of the endoplasmic reticulum
Auteurs : Svante P Bo ; Bheem M. Bhat ; William S. M. Wold ; Per A. PetersonSource :
- Cell [ 0092-8674 ] ; 1987.
English descriptors
- Teeft :
- Adenovirus, Amino, Amino acids, Andersson, Antigen, Biol, Carbohydrate moieties, Cell biol, Cell surface, Chase period, Coding assignment, Complex formation, Cytoplasmic, Cytoplasmic domains, Cytoplasmic segments, Cytoplasmic tail, Cytoplasmic tails, Endo, Endoplasmic, Endoplasmic reticulum, Experimental procedures, Fetal calf serum, Flow cytofluorometry, Free luminal domain, Glycoprotein, Glycoprotein fractions, Hela, Hela cells, Human adenoviruses, Human class, Human receptor, Indirect immunofluorescence staining, Indirect immunoprecipitation, Intracellular, Intracellular localization, Intracellular transport, Intraluminal domain, Latter case, Luminal, Luminal domain, Major histocompatibility, Membrane proteins, Monoclonal, Monoclonal antibody, Mutant, Mutant adenoviruses, Mutant protein, Mutant proteins, Mutant viruses, Nucleotide, Nucleotide sequence, Persson, Present study, Previous studies, Protein, Rabbit antiserum, Reticulum, Sequence motifs, Severinsson, Short sequence, Signal sequence, Subcellular, Subcellular fractionation, Termination codon, Transferrin receptor, Transplantation antigens, Viral, Viral protein, Xbal linker, Xenopus laevis oocytes.
Abstract
Abstract: The E19 protein of adenoviruses is a transmembrane protein that abrogates the intracellular transport of class I antigens by forming complexes with them in the ER. We show here that the E19 protein is retained in the ER even in the absence of class I antigens. To define the region conferring residency in the ER, we examined two mutant forms of the viral protein. A 5 amino acid extension of the 15-membered cytoplasmic tail of the protein reduces its interaction with class I antigens but does not change its intracellular distribution. Shortening the tail to 7 amino acids also diminishes the affinity for class I antigens; however, this mutant E19 protein becomes transported to the cell surface. Thus, we concluded that a small stretch of amino acids exposed on the cytoplasmic side of the ER membrane is responsible for the retention of the E19 protein in the ER.
Url:
DOI: 10.1016/0092-8674(87)90226-1
Links to Exploration step
ISTEX:901672806490C5AA4CBEF9886360F210CE727510Le document en format XML
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Bhat</name><affiliations><json:string>Institute for Molecular Virology Saint Louis University School of Medicine St. Louis, Missouri 63110 USA</json:string></affiliations></json:item><json:item><name>William S.M. Wold</name><affiliations><json:string>Institute for Molecular Virology Saint Louis University School of Medicine St. Louis, Missouri 63110 USA</json:string></affiliations></json:item><json:item><name>Per A. Peterson</name><affiliations><json:string>Department of Cell Research University of Uppsala S-751 24 Uppsala, Sweden</json:string><json:string>‡ Present address: Department of Immunology, Research Institute of Scripps Clinic, 10666 N. 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Thus, we concluded that a small stretch of amino acids exposed on the cytoplasmic side of the ER membrane is responsible for the retention of the E19 protein in the ER.</abstract><qualityIndicators><score>8.788</score><pdfWordCount>5205</pdfWordCount><pdfCharCount>33440</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>7</pdfPageCount><pdfPageSize>576 x 828 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>149</abstractWordCount><abstractCharCount>879</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>A short sequence in the COOH-terminus makes an adenovirus membrane glycoprotein a resident of the endoplasmic reticulum</title><pmid><json:string>2954653</json:string></pmid><pii><json:string>0092-8674(87)90226-1</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Proc. Natl. Acad. Sci. 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Section</json:string><json:string>S. M. Wold</json:string><json:string>S. Broome</json:string><json:string>Hugo Fellner-Feldegg</json:string><json:string>Eva Ahlstrom</json:string><json:string>Jutta Buxtorf</json:string><json:string>Erik Fries</json:string><json:string>La Jolla</json:string><json:string>Per A. Peterson</json:string></persName><placeName><json:string>Sweden</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Both et al., 1983a, 1983b</json:string><json:string>Tanaka et al., 1985</json:string><json:string>Herisse et al., 1980</json:string><json:string>Leonard et al., 1984</json:string><json:string>Deutscher et al., 1985</json:string><json:string>Andersson et al., 1985</json:string><json:string>Bhat et al., 1986</json:string><json:string>Hayman and Crumpton, 1972</json:string><json:string>Nikaido et al., 1984</json:string><json:string>Brands et al., 1985</json:string><json:string>Burgert and Kvist, 1985</json:string><json:string>Andersson et al. 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Torrey Pines Road, La Jolla, California 92037.</affiliation></author><idno type="istex">901672806490C5AA4CBEF9886360F210CE727510</idno><idno type="ark">ark:/67375/6H6-9KXFHQ42-P</idno><idno type="DOI">10.1016/0092-8674(87)90226-1</idno><idno type="PII">0092-8674(87)90226-1</idno></analytic><monogr><title level="j">Cell</title><title level="j" type="abbrev">CELL</title><idno type="pISSN">0092-8674</idno><idno type="PII">S0092-8674(00)X0246-2</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1987"></date><biblScope unit="volume">50</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="311">311</biblScope><biblScope unit="page" to="317">317</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1987</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: The E19 protein of adenoviruses is a transmembrane protein that abrogates the intracellular transport of class I antigens by forming complexes with them in the ER. We show here that the E19 protein is retained in the ER even in the absence of class I antigens. To define the region conferring residency in the ER, we examined two mutant forms of the viral protein. A 5 amino acid extension of the 15-membered cytoplasmic tail of the protein reduces its interaction with class I antigens but does not change its intracellular distribution. Shortening the tail to 7 amino acids also diminishes the affinity for class I antigens; however, this mutant E19 protein becomes transported to the cell surface. Thus, we concluded that a small stretch of amino acids exposed on the cytoplasmic side of the ER membrane is responsible for the retention of the E19 protein in the ER.</p></abstract></profileDesc><revisionDesc><change when="1987-04-28">Modified</change><change when="1987">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-9KXFHQ42-P/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>CELL</jid><aid>87902261</aid><ce:pii>0092-8674(87)90226-1</ce:pii><ce:doi>10.1016/0092-8674(87)90226-1</ce:doi><ce:copyright type="unknown" year="1987"></ce:copyright></item-info><head><ce:dochead><ce:textfn>Article</ce:textfn></ce:dochead><ce:title>A short sequence in the COOH-terminus makes an adenovirus membrane glycoprotein a resident of the endoplasmic reticulum</ce:title><ce:author-group><ce:author><ce:given-name>Svante</ce:given-name><ce:surname>Pääbo</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>★</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Bheem M.</ce:given-name><ce:surname>Bhat</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>†</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>William S.M.</ce:given-name><ce:surname>Wold</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>†</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Per A.</ce:given-name><ce:surname>Peterson</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>★</ce:sup></ce:cross-ref><ce:cross-ref refid="FN1"><ce:sup>‡</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Department of Cell Research University of Uppsala S-751 24 Uppsala, Sweden</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>Institute for Molecular Virology Saint Louis University School of Medicine St. Louis, Missouri 63110 USA</ce:textfn></ce:affiliation><ce:footnote id="FN1"><ce:label>‡</ce:label><ce:note-para>Present address: Department of Immunology, Research Institute of Scripps Clinic, 10666 N. Torrey Pines Road, La Jolla, California 92037.</ce:note-para></ce:footnote></ce:author-group><ce:date-received day="24" month="2" year="1987"></ce:date-received><ce:date-revised day="28" month="4" year="1987"></ce:date-revised><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>The E19 protein of adenoviruses is a transmembrane protein that abrogates the intracellular transport of class I antigens by forming complexes with them in the ER. We show here that the E19 protein is retained in the ER even in the absence of class I antigens. To define the region conferring residency in the ER, we examined two mutant forms of the viral protein. A 5 amino acid extension of the 15-membered cytoplasmic tail of the protein reduces its interaction with class I antigens but does not change its intracellular distribution. Shortening the tail to 7 amino acids also diminishes the affinity for class I antigens; however, this mutant E19 protein becomes transported to the cell surface. Thus, we concluded that a small stretch of amino acids exposed on the cytoplasmic side of the ER membrane is responsible for the retention of the E19 protein in the ER.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>A short sequence in the COOH-terminus makes an adenovirus membrane glycoprotein a resident of the endoplasmic reticulum</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>A short sequence in the COOH-terminus makes an adenovirus membrane glycoprotein a resident of the endoplasmic reticulum</title></titleInfo><name type="personal"><namePart type="given">Svante</namePart><namePart type="family">Pääbo</namePart><affiliation>Department of Cell Research University of Uppsala S-751 24 Uppsala, Sweden</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Bheem M.</namePart><namePart type="family">Bhat</namePart><affiliation>Institute for Molecular Virology Saint Louis University School of Medicine St. Louis, Missouri 63110 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">William S.M.</namePart><namePart type="family">Wold</namePart><affiliation>Institute for Molecular Virology Saint Louis University School of Medicine St. Louis, Missouri 63110 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Per A.</namePart><namePart type="family">Peterson</namePart><affiliation>Department of Cell Research University of Uppsala S-751 24 Uppsala, Sweden</affiliation><affiliation>‡ Present address: Department of Immunology, Research Institute of Scripps Clinic, 10666 N. Torrey Pines Road, La Jolla, California 92037.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1987</dateIssued><dateModified encoding="w3cdtf">1987-04-28</dateModified><copyrightDate encoding="w3cdtf">1987</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: The E19 protein of adenoviruses is a transmembrane protein that abrogates the intracellular transport of class I antigens by forming complexes with them in the ER. We show here that the E19 protein is retained in the ER even in the absence of class I antigens. To define the region conferring residency in the ER, we examined two mutant forms of the viral protein. A 5 amino acid extension of the 15-membered cytoplasmic tail of the protein reduces its interaction with class I antigens but does not change its intracellular distribution. Shortening the tail to 7 amino acids also diminishes the affinity for class I antigens; however, this mutant E19 protein becomes transported to the cell surface. Thus, we concluded that a small stretch of amino acids exposed on the cytoplasmic side of the ER membrane is responsible for the retention of the E19 protein in the ER.</abstract><note type="content">Section title: Article</note><relatedItem type="host"><titleInfo><title>Cell</title></titleInfo><titleInfo type="abbreviated"><title>CELL</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1987</dateIssued></originInfo><identifier type="ISSN">0092-8674</identifier><identifier type="PII">S0092-8674(00)X0246-2</identifier><part><date>1987</date><detail type="volume"><number>50</number><caption>vol.</caption></detail><detail type="issue"><number>2</number><caption>no.</caption></detail><extent unit="issue-pages"><start>147</start><end>325</end></extent><extent unit="pages"><start>311</start><end>317</end></extent></part></relatedItem><identifier type="istex">901672806490C5AA4CBEF9886360F210CE727510</identifier><identifier type="ark">ark:/67375/6H6-9KXFHQ42-P</identifier><identifier type="DOI">10.1016/0092-8674(87)90226-1</identifier><identifier type="PII">0092-8674(87)90226-1</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-9KXFHQ42-P/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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