Vps13 is required for the packaging of the ER into autophagosomes during ER-phagy.
Identifieur interne : 000040 ( Main/Corpus ); précédent : 000039; suivant : 000041Vps13 is required for the packaging of the ER into autophagosomes during ER-phagy.
Auteurs : Shuliang Chen ; Muriel Mari ; Smriti Parashar ; Dongmei Liu ; Yixian Cui ; Fulvio Reggiori ; Peter J. Novick ; Susan Ferro-NovickSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2020.
English descriptors
- KwdEn :
- Autophagosomes (metabolism), Autophagy (MeSH), Cell Line (MeSH), Endoplasmic Reticulum (genetics), Endoplasmic Reticulum (metabolism), Endosomes (genetics), Endosomes (metabolism), Humans (MeSH), Saccharomyces cerevisiae (cytology), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism).
- MESH :
- chemical , genetics : Saccharomyces cerevisiae Proteins.
- cytology : Saccharomyces cerevisiae.
- genetics : Endoplasmic Reticulum, Endosomes, Saccharomyces cerevisiae.
- metabolism : Autophagosomes, Endoplasmic Reticulum, Endosomes, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins.
- Autophagy, Cell Line, Humans.
Abstract
Endoplasmic reticulum (ER) macroautophagy (hereafter called ER-phagy) uses autophagy receptors to selectively degrade ER domains in response to starvation or the accumulation of aggregation-prone proteins. Autophagy receptors package the ER into autophagosomes by binding to the ubiquitin-like yeast protein Atg8 (LC3 in mammals), which is needed for autophagosome formation. In budding yeast, cortical and cytoplasmic ER-phagy requires the autophagy receptor Atg40. While different ER autophagy receptors have been identified, little is known about other components of the ER-phagy machinery. In an effort to identify these components, we screened the genome-wide library of viable yeast deletion mutants for defects in the degradation of cortical ER following treatment with rapamycin, a drug that mimics starvation. Among the mutants we identified was vps13Δ. While yeast has one gene that encodes the phospholipid transporter VPS13, humans have four vacuolar protein-sorting (VPS) protein 13 isoforms. Mutations in all four human isoforms have been linked to different neurological disorders, including Parkinson's disease. Our findings have shown that Vps13 acts after Atg40 engages the autophagy machinery. Vps13 resides at contact sites between the ER and several organelles, including late endosomes. In the absence of Vps13, the cortical ER marker Rtn1 accumulated at late endosomes, and a dramatic decrease in ER packaging into autophagosomes was observed. Together, these studies suggest a role for Vps13 in the sequestration of the ER into autophagosomes at late endosomes. These observations may have important implications for understanding Parkinson's and other neurological diseases.
DOI: 10.1073/pnas.2008923117
PubMed: 32690699
PubMed Central: PMC7414049
Links to Exploration step
pubmed:32690699Le document en format XML
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Novick</name><affiliation><nlm:affiliation>Department of Cellular and Molecular Medicine, University of California San Diego, La Jolla, CA 92093-0668; pnovick@ucsd.edu sfnovick@ucsd.edu.</nlm:affiliation></affiliation></author><author><name sortKey="Ferro Novick, Susan" sort="Ferro Novick, Susan" uniqKey="Ferro Novick S" first="Susan" last="Ferro-Novick">Susan Ferro-Novick</name><affiliation><nlm:affiliation>Department of Cellular and Molecular Medicine, University of California San Diego, La Jolla, CA 92093-0668; pnovick@ucsd.edu sfnovick@ucsd.edu.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2020">2020</date><idno type="RBID">pubmed:32690699</idno><idno type="pmid">32690699</idno><idno type="doi">10.1073/pnas.2008923117</idno><idno type="pmc">PMC7414049</idno><idno type="wicri:Area/Main/Corpus">000040</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000040</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Vps13 is required for the packaging of the ER into autophagosomes during ER-phagy.</title><author><name sortKey="Chen, Shuliang" sort="Chen, Shuliang" uniqKey="Chen S" first="Shuliang" last="Chen">Shuliang Chen</name><affiliation><nlm:affiliation>Department of Cellular and Molecular Medicine, University of California San Diego, La Jolla, CA 92093-0668.</nlm:affiliation></affiliation></author><author><name sortKey="Mari, Muriel" sort="Mari, Muriel" uniqKey="Mari M" first="Muriel" last="Mari">Muriel Mari</name><affiliation><nlm:affiliation>Department of Biomedical Sciences of Cells and Systems, University of Groningen, University Medical Center Groningen, 9713 AV Groningen, The Netherlands.</nlm:affiliation></affiliation></author><author><name sortKey="Parashar, Smriti" sort="Parashar, Smriti" uniqKey="Parashar S" first="Smriti" last="Parashar">Smriti Parashar</name><affiliation><nlm:affiliation>Department of Cellular and Molecular Medicine, University of California San Diego, La Jolla, CA 92093-0668.</nlm:affiliation></affiliation></author><author><name sortKey="Liu, Dongmei" sort="Liu, Dongmei" uniqKey="Liu D" first="Dongmei" last="Liu">Dongmei Liu</name><affiliation><nlm:affiliation>Department of Cellular and Molecular Medicine, University of California San Diego, La Jolla, CA 92093-0668.</nlm:affiliation></affiliation></author><author><name sortKey="Cui, Yixian" sort="Cui, Yixian" uniqKey="Cui Y" first="Yixian" last="Cui">Yixian Cui</name><affiliation><nlm:affiliation>Department of Cellular and Molecular Medicine, University of California San Diego, La Jolla, CA 92093-0668.</nlm:affiliation></affiliation></author><author><name sortKey="Reggiori, Fulvio" sort="Reggiori, Fulvio" uniqKey="Reggiori F" first="Fulvio" last="Reggiori">Fulvio Reggiori</name><affiliation><nlm:affiliation>Department of Biomedical Sciences of Cells and Systems, University of Groningen, University Medical Center Groningen, 9713 AV Groningen, The Netherlands.</nlm:affiliation></affiliation></author><author><name sortKey="Novick, Peter J" sort="Novick, Peter J" uniqKey="Novick P" first="Peter J" last="Novick">Peter J. Novick</name><affiliation><nlm:affiliation>Department of Cellular and Molecular Medicine, University of California San Diego, La Jolla, CA 92093-0668; pnovick@ucsd.edu sfnovick@ucsd.edu.</nlm:affiliation></affiliation></author><author><name sortKey="Ferro Novick, Susan" sort="Ferro Novick, Susan" uniqKey="Ferro Novick S" first="Susan" last="Ferro-Novick">Susan Ferro-Novick</name><affiliation><nlm:affiliation>Department of Cellular and Molecular Medicine, University of California San Diego, La Jolla, CA 92093-0668; pnovick@ucsd.edu sfnovick@ucsd.edu.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="eISSN">1091-6490</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Autophagosomes (metabolism)</term><term>Autophagy (MeSH)</term><term>Cell Line (MeSH)</term><term>Endoplasmic Reticulum (genetics)</term><term>Endoplasmic Reticulum (metabolism)</term><term>Endosomes (genetics)</term><term>Endosomes (metabolism)</term><term>Humans (MeSH)</term><term>Saccharomyces cerevisiae (cytology)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (genetics)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Endoplasmic Reticulum</term><term>Endosomes</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Autophagosomes</term><term>Endoplasmic Reticulum</term><term>Endosomes</term><term>Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Autophagy</term><term>Cell Line</term><term>Humans</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Endoplasmic reticulum (ER) macroautophagy (hereafter called ER-phagy) uses autophagy receptors to selectively degrade ER domains in response to starvation or the accumulation of aggregation-prone proteins. Autophagy receptors package the ER into autophagosomes by binding to the ubiquitin-like yeast protein Atg8 (LC3 in mammals), which is needed for autophagosome formation. In budding yeast, cortical and cytoplasmic ER-phagy requires the autophagy receptor Atg40. While different ER autophagy receptors have been identified, little is known about other components of the ER-phagy machinery. In an effort to identify these components, we screened the genome-wide library of viable yeast deletion mutants for defects in the degradation of cortical ER following treatment with rapamycin, a drug that mimics starvation. Among the mutants we identified was <i>vps13</i>Δ. While yeast has one gene that encodes the phospholipid transporter <i>VPS13</i>, humans have four vacuolar protein-sorting (VPS) protein 13 isoforms. Mutations in all four human isoforms have been linked to different neurological disorders, including Parkinson's disease. Our findings have shown that Vps13 acts after Atg40 engages the autophagy machinery. Vps13 resides at contact sites between the ER and several organelles, including late endosomes. In the absence of Vps13, the cortical ER marker Rtn1 accumulated at late endosomes, and a dramatic decrease in ER packaging into autophagosomes was observed. Together, these studies suggest a role for Vps13 in the sequestration of the ER into autophagosomes at late endosomes. These observations may have important implications for understanding Parkinson's and other neurological diseases.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">32690699</PMID><DateCompleted><Year>2020</Year><Month>09</Month><Day>30</Day></DateCompleted><DateRevised><Year>2020</Year><Month>11</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1091-6490</ISSN><JournalIssue CitedMedium="Internet"><Volume>117</Volume><Issue>31</Issue><PubDate><Year>2020</Year><Month>08</Month><Day>04</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc Natl Acad Sci U S A</ISOAbbreviation></Journal><ArticleTitle>Vps13 is required for the packaging of the ER into autophagosomes during ER-phagy.</ArticleTitle><Pagination><MedlinePgn>18530-18539</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.2008923117</ELocationID><Abstract><AbstractText>Endoplasmic reticulum (ER) macroautophagy (hereafter called ER-phagy) uses autophagy receptors to selectively degrade ER domains in response to starvation or the accumulation of aggregation-prone proteins. Autophagy receptors package the ER into autophagosomes by binding to the ubiquitin-like yeast protein Atg8 (LC3 in mammals), which is needed for autophagosome formation. In budding yeast, cortical and cytoplasmic ER-phagy requires the autophagy receptor Atg40. While different ER autophagy receptors have been identified, little is known about other components of the ER-phagy machinery. In an effort to identify these components, we screened the genome-wide library of viable yeast deletion mutants for defects in the degradation of cortical ER following treatment with rapamycin, a drug that mimics starvation. Among the mutants we identified was <i>vps13</i>Δ. While yeast has one gene that encodes the phospholipid transporter <i>VPS13</i>, humans have four vacuolar protein-sorting (VPS) protein 13 isoforms. Mutations in all four human isoforms have been linked to different neurological disorders, including Parkinson's disease. Our findings have shown that Vps13 acts after Atg40 engages the autophagy machinery. Vps13 resides at contact sites between the ER and several organelles, including late endosomes. In the absence of Vps13, the cortical ER marker Rtn1 accumulated at late endosomes, and a dramatic decrease in ER packaging into autophagosomes was observed. Together, these studies suggest a role for Vps13 in the sequestration of the ER into autophagosomes at late endosomes. These observations may have important implications for understanding Parkinson's and other neurological diseases.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Shuliang</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Cellular and Molecular Medicine, University of California San Diego, La Jolla, CA 92093-0668.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mari</LastName><ForeName>Muriel</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Biomedical Sciences of Cells and Systems, University of Groningen, University Medical Center Groningen, 9713 AV Groningen, The Netherlands.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Parashar</LastName><ForeName>Smriti</ForeName><Initials>S</Initials><Identifier Source="ORCID">0000-0002-6348-2612</Identifier><AffiliationInfo><Affiliation>Department of Cellular and Molecular Medicine, University of California San Diego, La Jolla, CA 92093-0668.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Dongmei</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Department of Cellular and Molecular Medicine, University of California San Diego, La Jolla, CA 92093-0668.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cui</LastName><ForeName>Yixian</ForeName><Initials>Y</Initials><Identifier Source="ORCID">0000-0001-8260-1421</Identifier><AffiliationInfo><Affiliation>Department of Cellular and Molecular Medicine, University of California San Diego, La Jolla, CA 92093-0668.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Reggiori</LastName><ForeName>Fulvio</ForeName><Initials>F</Initials><Identifier Source="ORCID">0000-0003-2652-2686</Identifier><AffiliationInfo><Affiliation>Department of Biomedical Sciences of Cells and Systems, University of Groningen, University Medical Center Groningen, 9713 AV Groningen, The Netherlands.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Novick</LastName><ForeName>Peter J</ForeName><Initials>PJ</Initials><AffiliationInfo><Affiliation>Department of Cellular and Molecular Medicine, University of California San Diego, La Jolla, CA 92093-0668; pnovick@ucsd.edu sfnovick@ucsd.edu.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ferro-Novick</LastName><ForeName>Susan</ForeName><Initials>S</Initials><Identifier Source="ORCID">0000-0001-8714-7352</Identifier><AffiliationInfo><Affiliation>Department of Cellular and Molecular Medicine, University of California San Diego, La Jolla, CA 92093-0668; pnovick@ucsd.edu sfnovick@ucsd.edu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 GM115422</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 GM114111</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 GM035370</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 GM082861</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R35 GM131681</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>07</Month><Day>20</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Proc Natl Acad Sci U S A</MedlineTA><NlmUniqueID>7505876</NlmUniqueID><ISSNLinking>0027-8424</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C110276">VPS13 protein, S cerevisiae</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000071182" MajorTopicYN="N">Autophagosomes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001343" MajorTopicYN="N">Autophagy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004721" MajorTopicYN="N">Endoplasmic Reticulum</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011992" MajorTopicYN="N">Endosomes</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">ER-phagy</Keyword><Keyword MajorTopicYN="Y">Vps13</Keyword><Keyword MajorTopicYN="Y">autophagy</Keyword><Keyword MajorTopicYN="Y">contact site</Keyword><Keyword MajorTopicYN="Y">lipid transporter</Keyword></KeywordList><CoiStatement>The authors declare no competing interest.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pmc-release"><Year>2021</Year><Month>01</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>7</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>10</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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