Regulated proteolysis of p62/SQSTM1 enables differential control of autophagy and nutrient sensing.
Identifieur interne : 000508 ( Main/Exploration ); précédent : 000507; suivant : 000509Regulated proteolysis of p62/SQSTM1 enables differential control of autophagy and nutrient sensing.
Auteurs : Julia Sanchez-Garrido [Royaume-Uni] ; Vanessa Sancho-Shimizu [Royaume-Uni] ; Avinash R. Shenoy [Royaume-Uni]Source :
- Science signaling [ 1937-9145 ] ; 2018.
Descripteurs français
- KwdFr :
- Autophagie (MeSH), Caspase 8 (génétique), Caspase 8 (métabolisme), Cellules HEK293 (MeSH), Cellules HeLa (MeSH), Complexe-1 cible mécanistique de la rapamycine (génétique), Complexe-1 cible mécanistique de la rapamycine (métabolisme), Démence frontotemporale (anatomopathologie), Démence frontotemporale (génétique), Démence frontotemporale (métabolisme), Humains (MeSH), Mutation (MeSH), Mâle (MeSH), Nutriments (métabolisme), Protéolyse (MeSH), Receptor-Interacting Protein Serine-Threonine Kinases (génétique), Receptor-Interacting Protein Serine-Threonine Kinases (métabolisme), Séquestosome-1 (génétique), Séquestosome-1 (métabolisme), Transduction du signal (MeSH).
- MESH :
- anatomopathologie : Démence frontotemporale.
- génétique : Caspase 8, Complexe-1 cible mécanistique de la rapamycine, Démence frontotemporale, Receptor-Interacting Protein Serine-Threonine Kinases, Séquestosome-1.
- métabolisme : Caspase 8, Complexe-1 cible mécanistique de la rapamycine, Démence frontotemporale, Nutriments, Receptor-Interacting Protein Serine-Threonine Kinases, Séquestosome-1.
- Autophagie, Cellules HEK293, Cellules HeLa, Humains, Mutation, Mâle, Protéolyse, Transduction du signal.
English descriptors
- KwdEn :
- Autophagy (MeSH), Caspase 8 (genetics), Caspase 8 (metabolism), Frontotemporal Dementia (genetics), Frontotemporal Dementia (metabolism), Frontotemporal Dementia (pathology), HEK293 Cells (MeSH), HeLa Cells (MeSH), Humans (MeSH), Male (MeSH), Mechanistic Target of Rapamycin Complex 1 (genetics), Mechanistic Target of Rapamycin Complex 1 (metabolism), Mutation (MeSH), Nutrients (metabolism), Proteolysis (MeSH), Receptor-Interacting Protein Serine-Threonine Kinases (genetics), Receptor-Interacting Protein Serine-Threonine Kinases (metabolism), Sequestosome-1 Protein (genetics), Sequestosome-1 Protein (metabolism), Signal Transduction (MeSH).
- MESH :
- chemical , genetics : Caspase 8, Mechanistic Target of Rapamycin Complex 1, Receptor-Interacting Protein Serine-Threonine Kinases, Sequestosome-1 Protein.
- chemical , metabolism : Caspase 8, Mechanistic Target of Rapamycin Complex 1, Receptor-Interacting Protein Serine-Threonine Kinases, Sequestosome-1 Protein.
- genetics : Frontotemporal Dementia.
- metabolism : Frontotemporal Dementia, Nutrients.
- pathology : Frontotemporal Dementia.
- Autophagy, HEK293 Cells, HeLa Cells, Humans, Male, Mutation, Proteolysis, Signal Transduction.
Abstract
The multidomain scaffold protein p62 (also called sequestosome-1) is involved in autophagy, antimicrobial immunity, and oncogenesis. Mutations in SQSTM1, which encodes p62, are linked to hereditary inflammatory conditions such as Paget's disease of the bone, frontotemporal dementia (FTD), amyotrophic lateral sclerosis, and distal myopathy with rimmed vacuoles. Here, we report that p62 was proteolytically trimmed by the protease caspase-8 into a stable protein, which we called p62TRM We found that p62TRM, but not full-length p62, was involved in nutrient sensing and homeostasis through the mechanistic target of rapamycin complex 1 (mTORC1). The kinase RIPK1 and caspase-8 controlled p62TRM production and thus promoted mTORC1 signaling. An FTD-linked p62 D329G polymorphism and a rare D329H variant could not be proteolyzed by caspase-8, and these noncleavable variants failed to activate mTORC1, thereby revealing the detrimental effect of these mutations. These findings on the role of p62TRM provide new insights into SQSTM1-linked diseases and mTORC1 signaling.
DOI: 10.1126/scisignal.aat6903
PubMed: 30514811
Affiliations:
Links toward previous steps (curation, corpus...)
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Shenoy</name><affiliation wicri:level="1"><nlm:affiliation>Section of Microbiology, Medical Research Council Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, UK. a.shenoy@imperial.ac.uk.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Section of Microbiology, Medical Research Council Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ</wicri:regionArea><wicri:noRegion>London SW7 2AZ</wicri:noRegion></affiliation></author></analytic><series><title level="j">Science signaling</title><idno type="eISSN">1937-9145</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Autophagy (MeSH)</term><term>Caspase 8 (genetics)</term><term>Caspase 8 (metabolism)</term><term>Frontotemporal Dementia (genetics)</term><term>Frontotemporal Dementia (metabolism)</term><term>Frontotemporal Dementia (pathology)</term><term>HEK293 Cells (MeSH)</term><term>HeLa Cells (MeSH)</term><term>Humans (MeSH)</term><term>Male (MeSH)</term><term>Mechanistic Target of Rapamycin Complex 1 (genetics)</term><term>Mechanistic Target of Rapamycin Complex 1 (metabolism)</term><term>Mutation (MeSH)</term><term>Nutrients (metabolism)</term><term>Proteolysis (MeSH)</term><term>Receptor-Interacting Protein Serine-Threonine Kinases (genetics)</term><term>Receptor-Interacting Protein Serine-Threonine Kinases (metabolism)</term><term>Sequestosome-1 Protein (genetics)</term><term>Sequestosome-1 Protein (metabolism)</term><term>Signal Transduction (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Autophagie (MeSH)</term><term>Caspase 8 (génétique)</term><term>Caspase 8 (métabolisme)</term><term>Cellules HEK293 (MeSH)</term><term>Cellules HeLa (MeSH)</term><term>Complexe-1 cible mécanistique de la rapamycine (génétique)</term><term>Complexe-1 cible mécanistique de la rapamycine (métabolisme)</term><term>Démence frontotemporale (anatomopathologie)</term><term>Démence frontotemporale (génétique)</term><term>Démence frontotemporale (métabolisme)</term><term>Humains (MeSH)</term><term>Mutation (MeSH)</term><term>Mâle (MeSH)</term><term>Nutriments (métabolisme)</term><term>Protéolyse (MeSH)</term><term>Receptor-Interacting Protein Serine-Threonine Kinases (génétique)</term><term>Receptor-Interacting Protein Serine-Threonine Kinases (métabolisme)</term><term>Séquestosome-1 (génétique)</term><term>Séquestosome-1 (métabolisme)</term><term>Transduction du signal (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Caspase 8</term><term>Mechanistic Target of Rapamycin Complex 1</term><term>Receptor-Interacting Protein Serine-Threonine Kinases</term><term>Sequestosome-1 Protein</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Caspase 8</term><term>Mechanistic Target of Rapamycin Complex 1</term><term>Receptor-Interacting Protein Serine-Threonine Kinases</term><term>Sequestosome-1 Protein</term></keywords><keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Démence frontotemporale</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Frontotemporal Dementia</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Caspase 8</term><term>Complexe-1 cible mécanistique de la rapamycine</term><term>Démence frontotemporale</term><term>Receptor-Interacting Protein Serine-Threonine Kinases</term><term>Séquestosome-1</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Frontotemporal Dementia</term><term>Nutrients</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Caspase 8</term><term>Complexe-1 cible mécanistique de la rapamycine</term><term>Démence frontotemporale</term><term>Nutriments</term><term>Receptor-Interacting Protein Serine-Threonine Kinases</term><term>Séquestosome-1</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Frontotemporal Dementia</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Autophagy</term><term>HEK293 Cells</term><term>HeLa Cells</term><term>Humans</term><term>Male</term><term>Mutation</term><term>Proteolysis</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Autophagie</term><term>Cellules HEK293</term><term>Cellules HeLa</term><term>Humains</term><term>Mutation</term><term>Mâle</term><term>Protéolyse</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The multidomain scaffold protein p62 (also called sequestosome-1) is involved in autophagy, antimicrobial immunity, and oncogenesis. Mutations in <i>SQSTM1</i>, which encodes p62, are linked to hereditary inflammatory conditions such as Paget's disease of the bone, frontotemporal dementia (FTD), amyotrophic lateral sclerosis, and distal myopathy with rimmed vacuoles. Here, we report that p62 was proteolytically trimmed by the protease caspase-8 into a stable protein, which we called p62<sup>TRM</sup> We found that p62<sup>TRM</sup>, but not full-length p62, was involved in nutrient sensing and homeostasis through the mechanistic target of rapamycin complex 1 (mTORC1). The kinase RIPK1 and caspase-8 controlled p62<sup>TRM</sup> production and thus promoted mTORC1 signaling. An FTD-linked p62 D329G polymorphism and a rare D329H variant could not be proteolyzed by caspase-8, and these noncleavable variants failed to activate mTORC1, thereby revealing the detrimental effect of these mutations. These findings on the role of p62<sup>TRM</sup> provide new insights into <i>SQSTM1</i>-linked diseases and mTORC1 signaling.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30514811</PMID><DateCompleted><Year>2019</Year><Month>10</Month><Day>25</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>09</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1937-9145</ISSN><JournalIssue CitedMedium="Internet"><Volume>11</Volume><Issue>559</Issue><PubDate><Year>2018</Year><Month>12</Month><Day>04</Day></PubDate></JournalIssue><Title>Science signaling</Title><ISOAbbreviation>Sci Signal</ISOAbbreviation></Journal><ArticleTitle>Regulated proteolysis of p62/SQSTM1 enables differential control of autophagy and nutrient sensing.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">eaat6903</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1126/scisignal.aat6903</ELocationID><Abstract><AbstractText>The multidomain scaffold protein p62 (also called sequestosome-1) is involved in autophagy, antimicrobial immunity, and oncogenesis. Mutations in <i>SQSTM1</i>, which encodes p62, are linked to hereditary inflammatory conditions such as Paget's disease of the bone, frontotemporal dementia (FTD), amyotrophic lateral sclerosis, and distal myopathy with rimmed vacuoles. Here, we report that p62 was proteolytically trimmed by the protease caspase-8 into a stable protein, which we called p62<sup>TRM</sup> We found that p62<sup>TRM</sup>, but not full-length p62, was involved in nutrient sensing and homeostasis through the mechanistic target of rapamycin complex 1 (mTORC1). The kinase RIPK1 and caspase-8 controlled p62<sup>TRM</sup> production and thus promoted mTORC1 signaling. An FTD-linked p62 D329G polymorphism and a rare D329H variant could not be proteolyzed by caspase-8, and these noncleavable variants failed to activate mTORC1, thereby revealing the detrimental effect of these mutations. These findings on the role of p62<sup>TRM</sup> provide new insights into <i>SQSTM1</i>-linked diseases and mTORC1 signaling.</AbstractText><CopyrightInformation>Copyright © 2018 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sanchez-Garrido</LastName><ForeName>Julia</ForeName><Initials>J</Initials><Identifier Source="ORCID">0000-0002-5847-4167</Identifier><AffiliationInfo><Affiliation>Section of Microbiology, Medical Research Council Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sancho-Shimizu</LastName><ForeName>Vanessa</ForeName><Initials>V</Initials><Identifier Source="ORCID">0000-0002-3519-0727</Identifier><AffiliationInfo><Affiliation>Section of Paediatrics, Imperial College London, London W21 PG, UK.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Section of Virology, Imperial College London, London W21 PG, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shenoy</LastName><ForeName>Avinash R</ForeName><Initials>AR</Initials><Identifier Source="ORCID">0000-0001-6228-9303</Identifier><AffiliationInfo><Affiliation>Section of Microbiology, Medical Research Council Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, UK. a.shenoy@imperial.ac.uk.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>MR/P028225/1</GrantID><Acronym>MRC_</Acronym><Agency>Medical Research Council</Agency><Country>United Kingdom</Country></Grant><Grant><GrantID>108246/Z/15/Z</GrantID><Acronym>WT_</Acronym><Agency>Wellcome Trust</Agency><Country>United Kingdom</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>12</Month><Day>04</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Sci Signal</MedlineTA><NlmUniqueID>101465400</NlmUniqueID><ISSNLinking>1945-0877</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C099718">SQSTM1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000071456">Sequestosome-1 Protein</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D000076222">Mechanistic Target of Rapamycin Complex 1</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="C506249">RIPK1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D053422">Receptor-Interacting Protein Serine-Threonine Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.-</RegistryNumber><NameOfSubstance UI="C505530">CASP8 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.-</RegistryNumber><NameOfSubstance UI="D053181">Caspase 8</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="CommentIn"><RefSource>Sci Signal. 2018 Dec 04;11(559):</RefSource><PMID Version="1">30514809</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D001343" MajorTopicYN="Y">Autophagy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053181" MajorTopicYN="N">Caspase 8</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D057180" MajorTopicYN="N">Frontotemporal Dementia</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="Y">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D057809" MajorTopicYN="N">HEK293 Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006367" MajorTopicYN="N">HeLa Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008297" MajorTopicYN="N">Male</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000076222" MajorTopicYN="N">Mechanistic Target of Rapamycin Complex 1</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="Y">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000078622" MajorTopicYN="N">Nutrients</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D059748" MajorTopicYN="N">Proteolysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053422" MajorTopicYN="N">Receptor-Interacting Protein Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000071456" MajorTopicYN="N">Sequestosome-1 Protein</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>12</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>12</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>10</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">30514811</ArticleId><ArticleId IdType="pii">11/559/eaat6903</ArticleId><ArticleId IdType="doi">10.1126/scisignal.aat6903</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Royaume-Uni</li></country></list><tree><country name="Royaume-Uni"><noRegion><name sortKey="Sanchez Garrido, Julia" sort="Sanchez Garrido, Julia" uniqKey="Sanchez Garrido J" first="Julia" last="Sanchez-Garrido">Julia Sanchez-Garrido</name></noRegion><name sortKey="Sancho Shimizu, Vanessa" sort="Sancho Shimizu, Vanessa" uniqKey="Sancho Shimizu V" first="Vanessa" last="Sancho-Shimizu">Vanessa Sancho-Shimizu</name><name sortKey="Sancho Shimizu, Vanessa" sort="Sancho Shimizu, Vanessa" uniqKey="Sancho Shimizu V" first="Vanessa" last="Sancho-Shimizu">Vanessa Sancho-Shimizu</name><name sortKey="Shenoy, Avinash R" sort="Shenoy, Avinash R" uniqKey="Shenoy A" first="Avinash R" last="Shenoy">Avinash R. 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