Evolving questions and paradigm shifts in endoplasmic-reticulum-associated degradation (ERAD)
ER‐associated degradation (ERAD) is a component of the protein quality control system, ensuring that aberrant polypeptides cannot transit through the secretory pathway. This is accomplished by a complex sequence of events in which unwanted proteins are selected in the ER and exported to the cytosol...
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Veröffentlicht in: | BioEssays 2003-09, Vol.25 (9), p.868-877 |
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description | ER‐associated degradation (ERAD) is a component of the protein quality control system, ensuring that aberrant polypeptides cannot transit through the secretory pathway. This is accomplished by a complex sequence of events in which unwanted proteins are selected in the ER and exported to the cytosol for degradation by the proteasome. Given that protein quality control can be essential for cell survival, it is not surprising that ERAD is linked to numerous disease states. Here we review the molecular mechanisms of ERAD, its role in metabolic regulation and biomedical implications, and the unanswered questions regarding this process. BioEssays 25:868–877, 2003. © 2003 Wiley Periodicals, Inc. |
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BioEssays 25:868–877, 2003. © 2003 Wiley Periodicals, Inc.</description><subject>Animals</subject><subject>Cell Membrane - metabolism</subject><subject>Cell Survival</subject><subject>Cysteine Endopeptidases - metabolism</subject><subject>Cytosol - metabolism</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Fungal Proteins - metabolism</subject><subject>Glycosylation</subject><subject>Humans</subject><subject>Models, Biological</subject><subject>Multienzyme Complexes - metabolism</subject><subject>Mutation</subject><subject>Proteasome Endopeptidase Complex</subject><subject>Protein Transport</subject><issn>0265-9247</issn><issn>1521-1878</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMlOwzAURS0EglLY8AEoKwRIAQ9JnCxLKQWEQCrjBll2_FwMGUqcFPh70gHYsfJbnHskH4R2CD4iGNNjZcG1F6N4BXVISIlPYh6vog6mUegnNOAbaNO5V4xxEtFgHW0QmrCY8KiDngfTMpvaYuy9N-BqWxbOk4X2JrKS2o5zz71YUzvPFh4Uupxk0uU29SuobdpkTe5L58rUyhq0p2HcjuRM4u0PRr3Tgy20ZmTmYHv5dtH92eCuf-5f3Qwv-r0rPw1ogn3OFDOgCA2wJBiMMYrhWPOQAZM0CoxksYkNGJUormMVSR1GGkuVhjjgNGVdtLfwTqpy_g-RW5dClskCysYJzsKYR5i34OECTKvSuQqMmFQ2l9WXIFjMYopZTDGP2cK7S2ujctB_6LJeC5AF8GEz-PpHJU4uBrc_Un-xsa6Gz9-NrN5ExBkPxeP1UDxdX5LLR_4gRuwb6LyQGA</recordid><startdate>200309</startdate><enddate>200309</enddate><creator>McCracken, Ardythe A.</creator><creator>Brodsky, Jeffrey L.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>200309</creationdate><title>Evolving questions and paradigm shifts in endoplasmic-reticulum-associated degradation (ERAD)</title><author>McCracken, Ardythe A. ; Brodsky, Jeffrey L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4290-73b3feb1240a10efffb308d753e3a264fa38f8fefb9b7d8b6ad56d0abc50472c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Animals</topic><topic>Cell Membrane - metabolism</topic><topic>Cell Survival</topic><topic>Cysteine Endopeptidases - metabolism</topic><topic>Cytosol - metabolism</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Fungal Proteins - metabolism</topic><topic>Glycosylation</topic><topic>Humans</topic><topic>Models, Biological</topic><topic>Multienzyme Complexes - metabolism</topic><topic>Mutation</topic><topic>Proteasome Endopeptidase Complex</topic><topic>Protein Transport</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>McCracken, Ardythe A.</creatorcontrib><creatorcontrib>Brodsky, Jeffrey L.</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>BioEssays</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>McCracken, Ardythe A.</au><au>Brodsky, Jeffrey L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evolving questions and paradigm shifts in endoplasmic-reticulum-associated degradation (ERAD)</atitle><jtitle>BioEssays</jtitle><addtitle>Bioessays</addtitle><date>2003-09</date><risdate>2003</risdate><volume>25</volume><issue>9</issue><spage>868</spage><epage>877</epage><pages>868-877</pages><issn>0265-9247</issn><eissn>1521-1878</eissn><abstract>ER‐associated degradation (ERAD) is a component of the protein quality control system, ensuring that aberrant polypeptides cannot transit through the secretory pathway. 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subjects | Animals Cell Membrane - metabolism Cell Survival Cysteine Endopeptidases - metabolism Cytosol - metabolism Endoplasmic Reticulum - metabolism Fungal Proteins - metabolism Glycosylation Humans Models, Biological Multienzyme Complexes - metabolism Mutation Proteasome Endopeptidase Complex Protein Transport |
title | Evolving questions and paradigm shifts in endoplasmic-reticulum-associated degradation (ERAD) |
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