Autophagy-independent LC3 function in vesicular traffic.
Identifieur interne : 001637 ( PubMed/Corpus ); précédent : 001636; suivant : 001638Autophagy-independent LC3 function in vesicular traffic.
Auteurs : Cornelis A M. De Haan ; Maurizio Molinari ; Fulvio ReggioriSource :
- Autophagy [ 1554-8635 ] ; 2010.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Microtubule-Associated Proteins.
- genetics : Coronaviridae.
- metabolism : Coronaviridae, Endoplasmic Reticulum, Microtubule-Associated Proteins, Transport Vesicles.
- physiology : Autophagy.
- Animals, Humans, Mice, Protein Folding.
Abstract
As protein folding is an imperfect process, the endoplasmic reticulum (ER) contains folding as well as ER-associated degradation (ERAD) machineries. In order to prevent premature interruption of folding, ERAD regulators and effectors such as EDEM1 and OS-9 are selectively cleared from the ER in so-called EDEMosomes to downregulate the degradative activity. The mechanism by which EDEM1 and OS-9 are subjected to rapid turnover, also known as ERAD tuning, shows similarities with, but is clearly distinct from, macroautophagy. Positive strand RNA coronaviruses (CoVs) such as the severe acute respiratory syndrome (SARS)-CoV and mouse hepatitis virus (MHV), induce in infected cells the formation of autophagosome-like, double-membrane vesicles (DMVs) to which their replication and transcription complexes are anchored. While it seems clear that CoVs hijack ER-derived host cell membranes for replication, the mechanism by which these DMVs are assembled has remained completely mysterious.
DOI: 10.4161/auto.6.7.13309
PubMed: 20814233
Links to Exploration step
pubmed:20814233Le document en format XML
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C.A.M.deHaan@uu.nl</nlm:affiliation></affiliation></author><author><name sortKey="Molinari, Maurizio" sort="Molinari, Maurizio" uniqKey="Molinari M" first="Maurizio" last="Molinari">Maurizio Molinari</name></author><author><name sortKey="Reggiori, Fulvio" sort="Reggiori, Fulvio" uniqKey="Reggiori F" first="Fulvio" last="Reggiori">Fulvio Reggiori</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2010">2010</date><idno type="RBID">pubmed:20814233</idno><idno type="pmid">20814233</idno><idno type="doi">10.4161/auto.6.7.13309</idno><idno type="wicri:Area/PubMed/Corpus">001637</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001637</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Autophagy-independent LC3 function in vesicular traffic.</title><author><name sortKey="De Haan, Cornelis A M" sort="De Haan, Cornelis A M" uniqKey="De Haan C" first="Cornelis A M" last="De Haan">Cornelis A M. De Haan</name><affiliation><nlm:affiliation>Virology Division, Department of Infectious Diseases and Immunology, Utrecht University, Utrecht, Netherlands. C.A.M.deHaan@uu.nl</nlm:affiliation></affiliation></author><author><name sortKey="Molinari, Maurizio" sort="Molinari, Maurizio" uniqKey="Molinari M" first="Maurizio" last="Molinari">Maurizio Molinari</name></author><author><name sortKey="Reggiori, Fulvio" sort="Reggiori, Fulvio" uniqKey="Reggiori F" first="Fulvio" last="Reggiori">Fulvio Reggiori</name></author></analytic><series><title level="j">Autophagy</title><idno type="eISSN">1554-8635</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Autophagy (physiology)</term><term>Coronaviridae (genetics)</term><term>Coronaviridae (metabolism)</term><term>Endoplasmic Reticulum (metabolism)</term><term>Humans</term><term>Mice</term><term>Microtubule-Associated Proteins (genetics)</term><term>Microtubule-Associated Proteins (metabolism)</term><term>Protein Folding</term><term>Transport Vesicles (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Microtubule-Associated Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Coronaviridae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Coronaviridae</term><term>Endoplasmic Reticulum</term><term>Microtubule-Associated Proteins</term><term>Transport Vesicles</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Autophagy</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Humans</term><term>Mice</term><term>Protein Folding</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">As protein folding is an imperfect process, the endoplasmic reticulum (ER) contains folding as well as ER-associated degradation (ERAD) machineries. In order to prevent premature interruption of folding, ERAD regulators and effectors such as EDEM1 and OS-9 are selectively cleared from the ER in so-called EDEMosomes to downregulate the degradative activity. The mechanism by which EDEM1 and OS-9 are subjected to rapid turnover, also known as ERAD tuning, shows similarities with, but is clearly distinct from, macroautophagy. Positive strand RNA coronaviruses (CoVs) such as the severe acute respiratory syndrome (SARS)-CoV and mouse hepatitis virus (MHV), induce in infected cells the formation of autophagosome-like, double-membrane vesicles (DMVs) to which their replication and transcription complexes are anchored. 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In order to prevent premature interruption of folding, ERAD regulators and effectors such as EDEM1 and OS-9 are selectively cleared from the ER in so-called EDEMosomes to downregulate the degradative activity. The mechanism by which EDEM1 and OS-9 are subjected to rapid turnover, also known as ERAD tuning, shows similarities with, but is clearly distinct from, macroautophagy. Positive strand RNA coronaviruses (CoVs) such as the severe acute respiratory syndrome (SARS)-CoV and mouse hepatitis virus (MHV), induce in infected cells the formation of autophagosome-like, double-membrane vesicles (DMVs) to which their replication and transcription complexes are anchored. 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