Human DnaJB6 Antiamyloid Chaperone Protects Yeast from Polyglutamine Toxicity Separately from Spatial Segregation of Aggregates.
Identifieur interne : 000857 ( Main/Exploration ); précédent : 000856; suivant : 000858Human DnaJB6 Antiamyloid Chaperone Protects Yeast from Polyglutamine Toxicity Separately from Spatial Segregation of Aggregates.
Auteurs : Jyotsna Kumar [États-Unis] ; Neila L. Kline [États-Unis] ; Daniel C. Masison [Danemark]Source :
- Molecular and cellular biology [ 1098-5549 ] ; 2018.
Descripteurs français
- KwdFr :
- Agrégats de protéines (physiologie), Amyloïde (métabolisme), Chaperons moléculaires (métabolisme), Humains (MeSH), Liaison aux protéines (physiologie), Peptides (métabolisme), Protéines de tissu nerveux (métabolisme), Protéines du choc thermique HSP40 (métabolisme), Protéines du choc thermique HSP70 (métabolisme), Saccharomyces cerevisiae (métabolisme), Séquence d'acides aminés (MeSH).
- MESH :
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Amyloid (metabolism), HSP40 Heat-Shock Proteins (metabolism), HSP70 Heat-Shock Proteins (metabolism), Humans (MeSH), Molecular Chaperones (metabolism), Nerve Tissue Proteins (metabolism), Peptides (metabolism), Protein Aggregates (physiology), Protein Binding (physiology), Saccharomyces cerevisiae (metabolism).
- MESH :
- chemical , metabolism : Amyloid, HSP40 Heat-Shock Proteins, HSP70 Heat-Shock Proteins, Molecular Chaperones, Nerve Tissue Proteins, Peptides.
- chemical , physiology : Protein Aggregates.
- metabolism : Saccharomyces cerevisiae.
- physiology : Protein Binding.
- Amino Acid Sequence, Humans.
Abstract
Polyglutamine (polyQ) aggregates are associated with pathology in protein-folding diseases and with toxicity in the yeast Saccharomyces cerevisiae Protection from polyQ toxicity in yeast by human DnaJB6 coincides with sequestration of aggregates. Gathering of misfolded proteins into deposition sites by protein quality control (PQC) factors has led to the view that PQC processes protect cells by spatially segregating toxic aggregates. Whether DnaJB6 depends on this machinery to sequester polyQ aggregates, if this sequestration is needed for DnaJB6 to protect cells, and the identity of the deposition site are unknown. Here, we found DnaJB6-driven deposits share characteristics with perivacuolar insoluble protein deposition sites (IPODs). Binding of DnaJB6 to aggregates was necessary, but not enough, for detoxification. Focal formation required a DnaJB6-Hsp70 interaction and actin, polyQ could be detoxified without sequestration, and segregation of aggregates alone was not protective. Our findings suggest DnaJB6 binds to smaller polyQ aggregates to block their toxicity. Assembly and segregation of detoxified aggregates are driven by an Hsp70- and actin-dependent process. Our findings show sequestration of aggregates is not the primary mechanism by which DnaJB6 suppresses toxicity and raise questions regarding how and when misfolded proteins are detoxified during spatial segregation.
DOI: 10.1128/MCB.00437-18
PubMed: 30224519
PubMed Central: PMC6234286
Affiliations:
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Kline</name><affiliation wicri:level="2"><nlm:affiliation>Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland</wicri:regionArea><placeName><region type="state">Maryland</region></placeName></affiliation></author><author><name sortKey="Masison, Daniel C" sort="Masison, Daniel C" uniqKey="Masison D" first="Daniel C" last="Masison">Daniel C. Masison</name><affiliation wicri:level="1"><nlm:affiliation>Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, USA danielmas@niddk.nih.gov.</nlm:affiliation><country wicri:rule="url">Danemark</country><wicri:regionArea>Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland</wicri:regionArea><wicri:noRegion>Maryland</wicri:noRegion></affiliation></author></analytic><series><title level="j">Molecular and cellular biology</title><idno type="eISSN">1098-5549</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Amyloid (metabolism)</term><term>HSP40 Heat-Shock Proteins (metabolism)</term><term>HSP70 Heat-Shock Proteins (metabolism)</term><term>Humans (MeSH)</term><term>Molecular Chaperones (metabolism)</term><term>Nerve Tissue Proteins (metabolism)</term><term>Peptides (metabolism)</term><term>Protein Aggregates (physiology)</term><term>Protein Binding (physiology)</term><term>Saccharomyces cerevisiae (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Agrégats de protéines (physiologie)</term><term>Amyloïde (métabolisme)</term><term>Chaperons moléculaires (métabolisme)</term><term>Humains (MeSH)</term><term>Liaison aux protéines (physiologie)</term><term>Peptides (métabolisme)</term><term>Protéines de tissu nerveux (métabolisme)</term><term>Protéines du choc thermique HSP40 (métabolisme)</term><term>Protéines du choc thermique HSP70 (métabolisme)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Amyloid</term><term>HSP40 Heat-Shock Proteins</term><term>HSP70 Heat-Shock Proteins</term><term>Molecular Chaperones</term><term>Nerve Tissue Proteins</term><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Protein Aggregates</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Amyloïde</term><term>Chaperons moléculaires</term><term>Peptides</term><term>Protéines de tissu nerveux</term><term>Protéines du choc thermique HSP40</term><term>Protéines du choc thermique HSP70</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Agrégats de protéines</term><term>Liaison aux protéines</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Protein Binding</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Humans</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Humains</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Polyglutamine (polyQ) aggregates are associated with pathology in protein-folding diseases and with toxicity in the yeast <i>Saccharomyces cerevisiae</i> Protection from polyQ toxicity in yeast by human DnaJB6 coincides with sequestration of aggregates. Gathering of misfolded proteins into deposition sites by protein quality control (PQC) factors has led to the view that PQC processes protect cells by spatially segregating toxic aggregates. Whether DnaJB6 depends on this machinery to sequester polyQ aggregates, if this sequestration is needed for DnaJB6 to protect cells, and the identity of the deposition site are unknown. Here, we found DnaJB6-driven deposits share characteristics with perivacuolar insoluble protein deposition sites (IPODs). Binding of DnaJB6 to aggregates was necessary, but not enough, for detoxification. Focal formation required a DnaJB6-Hsp70 interaction and actin, polyQ could be detoxified without sequestration, and segregation of aggregates alone was not protective. Our findings suggest DnaJB6 binds to smaller polyQ aggregates to block their toxicity. Assembly and segregation of detoxified aggregates are driven by an Hsp70- and actin-dependent process. Our findings show sequestration of aggregates is not the primary mechanism by which DnaJB6 suppresses toxicity and raise questions regarding how and when misfolded proteins are detoxified during spatial segregation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30224519</PMID><DateCompleted><Year>2019</Year><Month>06</Month><Day>17</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>17</Day></DateRevised><Article PubModel="Electronic-Print"><Journal><ISSN IssnType="Electronic">1098-5549</ISSN><JournalIssue CitedMedium="Internet"><Volume>38</Volume><Issue>23</Issue><PubDate><Year>2018</Year><Month>12</Month><Day>01</Day></PubDate></JournalIssue><Title>Molecular and cellular biology</Title><ISOAbbreviation>Mol Cell Biol</ISOAbbreviation></Journal><ArticleTitle>Human DnaJB6 Antiamyloid Chaperone Protects Yeast from Polyglutamine Toxicity Separately from Spatial Segregation of Aggregates.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">e00437-18</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1128/MCB.00437-18</ELocationID><Abstract><AbstractText>Polyglutamine (polyQ) aggregates are associated with pathology in protein-folding diseases and with toxicity in the yeast <i>Saccharomyces cerevisiae</i> Protection from polyQ toxicity in yeast by human DnaJB6 coincides with sequestration of aggregates. Gathering of misfolded proteins into deposition sites by protein quality control (PQC) factors has led to the view that PQC processes protect cells by spatially segregating toxic aggregates. Whether DnaJB6 depends on this machinery to sequester polyQ aggregates, if this sequestration is needed for DnaJB6 to protect cells, and the identity of the deposition site are unknown. Here, we found DnaJB6-driven deposits share characteristics with perivacuolar insoluble protein deposition sites (IPODs). Binding of DnaJB6 to aggregates was necessary, but not enough, for detoxification. Focal formation required a DnaJB6-Hsp70 interaction and actin, polyQ could be detoxified without sequestration, and segregation of aggregates alone was not protective. Our findings suggest DnaJB6 binds to smaller polyQ aggregates to block their toxicity. Assembly and segregation of detoxified aggregates are driven by an Hsp70- and actin-dependent process. Our findings show sequestration of aggregates is not the primary mechanism by which DnaJB6 suppresses toxicity and raise questions regarding how and when misfolded proteins are detoxified during spatial segregation.</AbstractText><CopyrightInformation>This is a work of the U.S. Government and is not subject to copyright protection in the United States. Foreign copyrights may apply.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y" EqualContrib="Y"><LastName>Kumar</LastName><ForeName>Jyotsna</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y" EqualContrib="Y"><LastName>Kline</LastName><ForeName>Neila L</ForeName><Initials>NL</Initials><AffiliationInfo><Affiliation>Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Masison</LastName><ForeName>Daniel C</ForeName><Initials>DC</Initials><AffiliationInfo><Affiliation>Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, USA danielmas@niddk.nih.gov.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052060">Research Support, N.I.H., Intramural</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>11</Month><Day>13</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Mol Cell Biol</MedlineTA><NlmUniqueID>8109087</NlmUniqueID><ISSNLinking>0270-7306</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000682">Amyloid</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C485565">DNAJB6 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D050956">HSP40 Heat-Shock 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MajorTopicYN="N">Amyloid</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D050956" MajorTopicYN="N">HSP40 Heat-Shock Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018840" MajorTopicYN="N">HSP70 Heat-Shock Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018832" MajorTopicYN="N">Molecular Chaperones</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009419" MajorTopicYN="N">Nerve Tissue Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D066329" MajorTopicYN="N">Protein Aggregates</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">DnaJB6</Keyword><Keyword MajorTopicYN="Y">Huntington's disease</Keyword><Keyword MajorTopicYN="Y">J-protein</Keyword><Keyword MajorTopicYN="Y">amyloid</Keyword><Keyword MajorTopicYN="Y">heat shock protein (HSP)</Keyword><Keyword MajorTopicYN="Y">molecular 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Kline</name></country><country name="Danemark"><noRegion><name sortKey="Masison, Daniel C" sort="Masison, Daniel C" uniqKey="Masison D" first="Daniel C" last="Masison">Daniel C. Masison</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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