A short sequence in the COOH-terminus makes an adenovirus membrane glycoprotein a resident of the endoplasmic reticulum
Identifieur interne : 001D28 ( Main/Exploration ); précédent : 001D27; suivant : 001D29A short sequence in the COOH-terminus makes an adenovirus membrane glycoprotein a resident of the endoplasmic reticulum
Auteurs : Svante P Bo [Suède] ; Bheem M. Bhat [États-Unis] ; William S. M. Wold [États-Unis] ; Per A. Peterson [Suède, États-Unis]Source :
- 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
Affiliations:
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Bhat</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Missouri (État)</region></placeName><wicri:cityArea>Institute for Molecular Virology Saint Louis University School of Medicine St. Louis</wicri:cityArea></affiliation></author><author><name sortKey="Wold, William S M" sort="Wold, William S M" uniqKey="Wold W" first="William S. M." last="Wold">William S. M. Wold</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Missouri (État)</region></placeName><wicri:cityArea>Institute for Molecular Virology Saint Louis University School of Medicine St. Louis</wicri:cityArea></affiliation></author><author><name sortKey="Peterson, Per A" sort="Peterson, Per A" uniqKey="Peterson P" first="Per A." last="Peterson">Per A. Peterson</name><affiliation wicri:level="1"><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Cell Research University of Uppsala S-751 24 Uppsala</wicri:regionArea></affiliation><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>‡ Present address: Department of Immunology, Research Institute of Scripps Clinic, 10666 N. Torrey Pines Road, La Jolla</wicri:cityArea></affiliation></author></analytic><monogr></monogr><series><title level="j">Cell</title><title level="j" type="abbrev">CELL</title><idno type="ISSN">0092-8674</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1987">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><idno type="ISSN">0092-8674</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0092-8674</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Adenovirus</term><term>Amino</term><term>Amino acids</term><term>Andersson</term><term>Antigen</term><term>Biol</term><term>Carbohydrate moieties</term><term>Cell biol</term><term>Cell surface</term><term>Chase period</term><term>Coding assignment</term><term>Complex formation</term><term>Cytoplasmic</term><term>Cytoplasmic domains</term><term>Cytoplasmic segments</term><term>Cytoplasmic tail</term><term>Cytoplasmic tails</term><term>Endo</term><term>Endoplasmic</term><term>Endoplasmic reticulum</term><term>Experimental procedures</term><term>Fetal calf serum</term><term>Flow cytofluorometry</term><term>Free luminal domain</term><term>Glycoprotein</term><term>Glycoprotein fractions</term><term>Hela</term><term>Hela cells</term><term>Human adenoviruses</term><term>Human class</term><term>Human receptor</term><term>Indirect immunofluorescence staining</term><term>Indirect immunoprecipitation</term><term>Intracellular</term><term>Intracellular localization</term><term>Intracellular transport</term><term>Intraluminal domain</term><term>Latter case</term><term>Luminal</term><term>Luminal domain</term><term>Major histocompatibility</term><term>Membrane proteins</term><term>Monoclonal</term><term>Monoclonal antibody</term><term>Mutant</term><term>Mutant adenoviruses</term><term>Mutant protein</term><term>Mutant proteins</term><term>Mutant viruses</term><term>Nucleotide</term><term>Nucleotide sequence</term><term>Persson</term><term>Present study</term><term>Previous studies</term><term>Protein</term><term>Rabbit antiserum</term><term>Reticulum</term><term>Sequence motifs</term><term>Severinsson</term><term>Short sequence</term><term>Signal sequence</term><term>Subcellular</term><term>Subcellular fractionation</term><term>Termination codon</term><term>Transferrin receptor</term><term>Transplantation antigens</term><term>Viral</term><term>Viral protein</term><term>Xbal linker</term><term>Xenopus laevis oocytes</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml: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.</div></front></TEI><affiliations><list><country><li>Suède</li><li>États-Unis</li></country><region><li>Californie</li><li>Missouri (État)</li></region></list><tree><country name="Suède"><noRegion><name sortKey="P Bo, Svante" sort="P Bo, Svante" uniqKey="P Bo S" first="Svante" last="P Bo">Svante P Bo</name></noRegion><name sortKey="Peterson, Per A" sort="Peterson, Per A" uniqKey="Peterson P" first="Per A." last="Peterson">Per A. Peterson</name></country><country name="États-Unis"><region name="Missouri (État)"><name sortKey="Bhat, Bheem M" sort="Bhat, Bheem M" uniqKey="Bhat B" first="Bheem M." last="Bhat">Bheem M. Bhat</name></region><name sortKey="Peterson, Per A" sort="Peterson, Per A" uniqKey="Peterson P" first="Per A." last="Peterson">Per A. Peterson</name><name sortKey="Wold, William S M" sort="Wold, William S M" uniqKey="Wold W" first="William S. M." last="Wold">William S. M. Wold</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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