A sequential model for peptide binding and transport by the transporters associated with antigen processing
Identifieur interne : 000348 ( France/Analysis ); précédent : 000347; suivant : 000349A sequential model for peptide binding and transport by the transporters associated with antigen processing
Auteurs : Peter M. Van Endert [France, États-Unis] ; Robert Tampé ; Thomas H. Meyer [France] ; Roland Tisch [France] ; Jean-François Bach [France] ; Hugh O. Mcdevitt [France]Source :
- Immunity [ 1074-7613 ] ; 1994.
English descriptors
- Teeft :
- Affinity, Amino, Amino acids, Androlewicz, Antigen processing, Assay, Assay buffer, Binding, Binding assays, Binding site, Cavitation buffer, Cdna, Competitor, Competitor peptide, Cresswell, Endoplasmic reticulum, Glycosylation, Glycosylation motif, High affinity, Histocompatibility, Insect cell microsomes, Insect cells, Microsome, Molar, Momburg, Overexpression system, Peptide, Peptide accumulation, Peptide affinity, Peptide binding, Peptide length, Peptide release, Peptide transport, Permeabilized cells, Protease inhibitors, Random peptide mixtures, Random peptides, Recombinant, Recombinant viruses, Reporter peptide, Reporter peptides, Retention system, Small molar, Specific binding, Tap1, Tap2, Tap2 fragment, Tap2 proteins, Tapi, Translocation, Transport assays, Transporter, Unpublished data, Vesicle, Western blots.
Abstract
Abstract: The TAP proteins translocate antigenic peptides into the endoplasmic reticulum. Investigation of the specificity of this process has been complicated by TAP-independent factors that influence the amount of peptide that accumulates in the ER in transport assays. We have developed an overexpression system in which binding of peptides to the TAP substrate-binding site and peptide transport by TAP can be quantified separately. Efficiency of peptide accumulation in the ER parallels affinity forthe TAP substrate-binding site, but can be modified by interaction with the glycosylation system within the ER and, probably, peptide efflux. Random peptide mixtures of 9–16 as display significantly higher affinity for the binding site than mixtures of shorter or longer peptides. Peptide binds to TAP heteromers in the absence of ATP and is released by the binding of ATP, suggesting a model for TAP function.
Url:
DOI: 10.1016/1074-7613(94)90091-4
Affiliations:
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ISTEX:947399A2A0140381422BBF942FD470029557451FLe document en format XML
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Van Endert</name><affiliation wicri:level="1"><country xml:lang="fr">France</country><wicri:regionArea>Institut National de la Santé et de la Recherche Médicale U25 161 rue de Sèvres 75743 Paris</wicri:regionArea></affiliation><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology and Immunology Stanford University School of Medicine Stanford, California 94305-5402</wicri:regionArea><wicri:noRegion>California 94305-5402</wicri:noRegion></affiliation></author><author><name sortKey="Tampe, Robert" sort="Tampe, Robert" uniqKey="Tampe R" first="Robert" last="Tampé">Robert Tampé</name><affiliation><wicri:noCountry code="no comma">Max Planck Institut für Biochemie 62152 Martinsried Federal Republic of Germany</wicri:noCountry></affiliation></author><author><name sortKey="Meyer, Thomas H" sort="Meyer, Thomas H" uniqKey="Meyer T" first="Thomas H." last="Meyer">Thomas H. Meyer</name><affiliation wicri:level="1"><country xml:lang="fr">France</country><wicri:regionArea>Institut National de la Santé et de la Recherche Médicale U25 161 rue de Sèvres 75743 Paris</wicri:regionArea></affiliation></author><author><name sortKey="Tisch, Roland" sort="Tisch, Roland" uniqKey="Tisch R" first="Roland" last="Tisch">Roland Tisch</name><affiliation wicri:level="1"><country xml:lang="fr">France</country><wicri:regionArea>Institut National de la Santé et de la Recherche Médicale U25 161 rue de Sèvres 75743 Paris</wicri:regionArea></affiliation></author><author><name sortKey="Bach, Jean Francois" sort="Bach, Jean Francois" uniqKey="Bach J" first="Jean-François" last="Bach">Jean-François Bach</name><affiliation wicri:level="1"><country xml:lang="fr">France</country><wicri:regionArea>Institut National de la Santé et de la Recherche Médicale U25 161 rue de Sèvres 75743 Paris</wicri:regionArea></affiliation></author><author><name sortKey="Mcdevitt, Hugh O" sort="Mcdevitt, Hugh O" uniqKey="Mcdevitt H" first="Hugh O." last="Mcdevitt">Hugh O. Mcdevitt</name><affiliation wicri:level="1"><country xml:lang="fr">France</country><wicri:regionArea>Institut National de la Santé et de la Recherche Médicale U25 161 rue de Sèvres 75743 Paris</wicri:regionArea></affiliation></author></analytic><monogr></monogr><series><title level="j">Immunity</title><title level="j" type="abbrev">IMMUNI</title><idno type="ISSN">1074-7613</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1994">1994</date><biblScope unit="volume">1</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="491">491</biblScope><biblScope unit="page" to="500">500</biblScope></imprint><idno type="ISSN">1074-7613</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1074-7613</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Affinity</term><term>Amino</term><term>Amino acids</term><term>Androlewicz</term><term>Antigen processing</term><term>Assay</term><term>Assay buffer</term><term>Binding</term><term>Binding assays</term><term>Binding site</term><term>Cavitation buffer</term><term>Cdna</term><term>Competitor</term><term>Competitor peptide</term><term>Cresswell</term><term>Endoplasmic reticulum</term><term>Glycosylation</term><term>Glycosylation motif</term><term>High affinity</term><term>Histocompatibility</term><term>Insect cell microsomes</term><term>Insect cells</term><term>Microsome</term><term>Molar</term><term>Momburg</term><term>Overexpression system</term><term>Peptide</term><term>Peptide accumulation</term><term>Peptide affinity</term><term>Peptide binding</term><term>Peptide length</term><term>Peptide release</term><term>Peptide transport</term><term>Permeabilized cells</term><term>Protease inhibitors</term><term>Random peptide mixtures</term><term>Random peptides</term><term>Recombinant</term><term>Recombinant viruses</term><term>Reporter peptide</term><term>Reporter peptides</term><term>Retention system</term><term>Small molar</term><term>Specific binding</term><term>Tap1</term><term>Tap2</term><term>Tap2 fragment</term><term>Tap2 proteins</term><term>Tapi</term><term>Translocation</term><term>Transport assays</term><term>Transporter</term><term>Unpublished data</term><term>Vesicle</term><term>Western blots</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The TAP proteins translocate antigenic peptides into the endoplasmic reticulum. Investigation of the specificity of this process has been complicated by TAP-independent factors that influence the amount of peptide that accumulates in the ER in transport assays. We have developed an overexpression system in which binding of peptides to the TAP substrate-binding site and peptide transport by TAP can be quantified separately. Efficiency of peptide accumulation in the ER parallels affinity forthe TAP substrate-binding site, but can be modified by interaction with the glycosylation system within the ER and, probably, peptide efflux. Random peptide mixtures of 9–16 as display significantly higher affinity for the binding site than mixtures of shorter or longer peptides. Peptide binds to TAP heteromers in the absence of ATP and is released by the binding of ATP, suggesting a model for TAP function.</div></front></TEI><affiliations><list><country><li>France</li><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Tampe, Robert" sort="Tampe, Robert" uniqKey="Tampe R" first="Robert" last="Tampé">Robert Tampé</name></noCountry><country name="France"><noRegion><name sortKey="Van Endert, Peter M" sort="Van Endert, Peter M" uniqKey="Van Endert P" first="Peter M." last="Van Endert">Peter M. Van Endert</name></noRegion><name sortKey="Bach, Jean Francois" sort="Bach, Jean Francois" uniqKey="Bach J" first="Jean-François" last="Bach">Jean-François Bach</name><name sortKey="Mcdevitt, Hugh O" sort="Mcdevitt, Hugh O" uniqKey="Mcdevitt H" first="Hugh O." last="Mcdevitt">Hugh O. Mcdevitt</name><name sortKey="Meyer, Thomas H" sort="Meyer, Thomas H" uniqKey="Meyer T" first="Thomas H." last="Meyer">Thomas H. 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