Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0015532
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dc.titleInterplay of substrate retention and export signals in endoplasmic reticulum quality control
dc.contributor.authorKawaguchi S.
dc.contributor.authorHsu C.-L.
dc.contributor.authorNg D.T.W.
dc.date.accessioned2020-03-18T05:50:46Z
dc.date.available2020-03-18T05:50:46Z
dc.date.issued2010
dc.identifier.citationKawaguchi S., Hsu C.-L., Ng D.T.W. (2010). Interplay of substrate retention and export signals in endoplasmic reticulum quality control. PLoS ONE 5 (11) : e15532. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0015532
dc.identifier.issn19326203
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/165597
dc.description.abstractBackground: Endoplasmic reticulum (ER) quality control mechanisms are part of a comprehensive system to manage cell stress. The flux of molecules is monitored to retain folding intermediates and target misfolded molecules to ER-associated degradation (ERAD) pathways. The mechanisms of sorting remain unclear. While some proteins are retained statically, the classical model substrate CPY* is found in COPII transport vesicles, suggesting a retrieval mechanism for retention. However, its management can be even more dynamic. If ERAD is saturated under stress, excess CPY* traffics to the vacuole for degradation. These observations suggest that misfolded proteins might display different signals for their management. Methodology/Principal Findings: Here, we report the existence of a functional ER exit signal in the pro-domain of CPY*. Compromising its integrity causes ER retention through exclusion from COPII vesicles. The signal co-exists with other signals used for retention and degradation. Physiologically, the export signal is important for stress tolerance. Disabling it converts a benign protein into one that is intrinsically cytotoxic. Conclusions/Significance: These data reveal the remarkable interplay between opposing signals embedded within ERAD substrate molecules and the mechanisms that decipher them. Our findings demonstrate the diversity of mechanisms deployed for protein quality control and maintenance of protein homeostasis. © 2010 Kawaguchi et al.
dc.publisherPublic Library of Science
dc.sourceUnpaywall 20200320
dc.subjectcycloheximide
dc.subjectglycan
dc.subjectglycopeptidase
dc.subjectmembrane protein
dc.subjectprotein CPY
dc.subjectunclassified drug
dc.subjectpolysaccharide
dc.subjectSaccharomyces cerevisiae protein
dc.subjectarticle
dc.subjectcontrolled study
dc.subjectcytotoxicity
dc.subjectendoplasmic reticulum
dc.subjectendoplasmic reticulum stress
dc.subjectenzyme substrate
dc.subjecthomeostasis
dc.subjectnonhuman
dc.subjectnuclear export signal
dc.subjectprotein degradation
dc.subjectprotein folding
dc.subjectprotein processing
dc.subjectquality control
dc.subjectsignal transduction
dc.subjecttransport vesicle
dc.subjectchemistry
dc.subjectfluorescence microscopy
dc.subjectgenetics
dc.subjectglycosylation
dc.subjectGolgi complex
dc.subjectmetabolism
dc.subjectmutation
dc.subjectprotein transport
dc.subjectSaccharomyces cerevisiae
dc.subjectsignal transduction
dc.subjectEndoplasmic Reticulum
dc.subjectGlycosylation
dc.subjectGolgi Apparatus
dc.subjectMicroscopy, Fluorescence
dc.subjectMutation
dc.subjectPolysaccharides
dc.subjectProtein Folding
dc.subjectProtein Processing, Post-Translational
dc.subjectProtein Transport
dc.subjectSaccharomyces cerevisiae
dc.subjectSaccharomyces cerevisiae Proteins
dc.subjectSignal Transduction
dc.typeArticle
dc.contributor.departmentBIOLOGY (NU)
dc.contributor.departmentDEPT OF PHARMACOLOGY
dc.description.doi10.1371/journal.pone.0015532
dc.description.sourcetitlePLoS ONE
dc.description.volume5
dc.description.issue11
dc.description.pagee15532
dc.published.statePublished
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