Post-proteasomal and proteasome-independent generation of MHC class I ligands
Identifieur interne : 002532 ( Main/Exploration ); précédent : 002531; suivant : 002533Post-proteasomal and proteasome-independent generation of MHC class I ligands
Auteurs : Peter Van Endert [France]Source :
- Cellular and Molecular Life Sciences [ 1420-682X ] ; 2011-05-01.
English descriptors
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Abstract
Abstract: Peptide ligands presented by MHC class I molecules are produced by intracellular proteolysis, which often involves multiple steps. Initial antigen degradation seems to rely almost invariably on the proteasome, although tripeptidyl peptidase II (TPP II) and insulin-degrading enzyme (IDE) may be able to substitute for the proteasome in rare cases. Recent evidence suggests that the net effect of cytosolic aminopeptidases is destruction of potential class I ligands, although a positive role in selected cases has been documented. This may apply particularly to the trimming of long precursors by TPP II. In contrast, trimming of ligand precursors in the endoplasmic reticulum is essential for the generation of suitable peptides and has a substantial impact on the repertoire of ligands presented. Trimming by the ER aminopeptidase (ERAP) enzymes most likely acts on free precursors and is adapted to the needs of class I molecules by way of a molecular ruler mechanism. Trimming by ERAP enzymes also occurs for cross-presented ligands, which can alternatively be processed in a special endosomal compartment by insulin-regulated aminopeptidase.
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DOI: 10.1007/s00018-011-0662-1
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Mol. Life Sci.</title><idno type="ISSN">1420-682X</idno><idno type="eISSN">1420-9071</idno><imprint><publisher>SP Birkhäuser Verlag Basel</publisher><pubPlace>Basel</pubPlace><date type="published" when="2011-05-01">2011-05-01</date><biblScope unit="volume">68</biblScope><biblScope unit="issue">9</biblScope><biblScope unit="page" from="1553">1553</biblScope><biblScope unit="page" to="1567">1567</biblScope></imprint><idno type="ISSN">1420-682X</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1420-682X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antigen processing</term><term>ERAP</term><term>IRAP</term><term>Insulin-degrading enzyme</term><term>MHC class I</term><term>Nardilysin</term><term>Peptidase</term><term>TPP II</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Peptide ligands presented by MHC class I molecules are produced by intracellular proteolysis, which often involves multiple steps. Initial antigen degradation seems to rely almost invariably on the proteasome, although tripeptidyl peptidase II (TPP II) and insulin-degrading enzyme (IDE) may be able to substitute for the proteasome in rare cases. Recent evidence suggests that the net effect of cytosolic aminopeptidases is destruction of potential class I ligands, although a positive role in selected cases has been documented. This may apply particularly to the trimming of long precursors by TPP II. In contrast, trimming of ligand precursors in the endoplasmic reticulum is essential for the generation of suitable peptides and has a substantial impact on the repertoire of ligands presented. Trimming by the ER aminopeptidase (ERAP) enzymes most likely acts on free precursors and is adapted to the needs of class I molecules by way of a molecular ruler mechanism. Trimming by ERAP enzymes also occurs for cross-presented ligands, which can alternatively be processed in a special endosomal compartment by insulin-regulated aminopeptidase.</div></front></TEI><affiliations><list><country><li>France</li></country><region><li>Île-de-France</li></region><settlement><li>Paris</li></settlement><orgName><li>Université Paris-Descartes</li></orgName></list><tree><country name="France"><region name="Île-de-France"><name sortKey="Van Endert, Peter" sort="Van Endert, Peter" uniqKey="Van Endert P" first="Peter" last="Van Endert">Peter Van Endert</name></region><name sortKey="Van Endert, Peter" sort="Van Endert, Peter" uniqKey="Van Endert P" first="Peter" last="Van Endert">Peter Van Endert</name><name sortKey="Van Endert, Peter" sort="Van Endert, Peter" uniqKey="Van Endert P" first="Peter" last="Van Endert">Peter Van Endert</name><name sortKey="Van Endert, Peter" sort="Van Endert, Peter" uniqKey="Van Endert P" first="Peter" last="Van Endert">Peter Van Endert</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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