The autophagy initiator ULK1 sensitizes AMPK to allosteric drugs.
Identifieur interne : 000586 ( PubMed/Corpus ); précédent : 000585; suivant : 000587The autophagy initiator ULK1 sensitizes AMPK to allosteric drugs.
Auteurs : Toby A. Dite ; Naomi X Y. Ling ; John W. Scott ; Ashfaqul Hoque ; Sandra Galic ; Benjamin L. Parker ; Kevin R W. Ngoei ; Christopher G. Langendorf ; Matthew T. O'Brien ; Mondira Kundu ; Benoit Viollet ; Gregory R. Steinberg ; Kei Sakamoto ; Bruce E. Kemp ; Jonathan S. OakhillSource :
- Nature communications [ 2041-1723 ] ; 2017.
Abstract
AMP-activated protein kinase (AMPK) is a metabolic stress-sensing enzyme responsible for maintaining cellular energy homeostasis. Activation of AMPK by salicylate and the thienopyridone A-769662 is critically dependent on phosphorylation of Ser108 in the β1 regulatory subunit. Here, we show a possible role for Ser108 phosphorylation in cell cycle regulation and promotion of pro-survival pathways in response to energy stress. We identify the autophagy initiator Unc-51-like kinase 1 (ULK1) as a β1-Ser108 kinase in cells. Cellular β1-Ser108 phosphorylation by ULK1 was dependent on AMPK β-subunit myristoylation, metabolic stress associated with elevated AMP/ATP ratio, and the intrinsic energy sensing capacity of AMPK; features consistent with an AMP-induced myristoyl switch mechanism. We further demonstrate cellular AMPK signaling independent of activation loop Thr172 phosphorylation, providing potential insight into physiological roles for Ser108 phosphorylation. These findings uncover new mechanisms by which AMPK could potentially maintain cellular energy homeostasis independently of Thr172 phosphorylation.AMPK is involved in sensing of metabolic stress. The authors show that the autophagy initiator ULK1 phosphorylates β1-Ser108 on the regulatory β1-subunit, sensitizing AMPK to allosteric drugs, and activates signaling pathways that appear independent of Thr172 phosphorylation in the kinase activation loop.
DOI: 10.1038/s41467-017-00628-y
PubMed: 28924239
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Kemp</name><affiliation><nlm:affiliation>Protein Chemistry & Metabolism, St Vincent's Institute of Medical Research, University of Melbourne, Melbourne, VIC, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Oakhill, Jonathan S" sort="Oakhill, Jonathan S" uniqKey="Oakhill J" first="Jonathan S" last="Oakhill">Jonathan S. Oakhill</name><affiliation><nlm:affiliation>Metabolic Signalling Laboratory, St Vincent's Institute of Medical Research, University of Melbourne, Melbourne, VIC, Australia. joakhill@svi.edu.au.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2017">2017</date><idno type="RBID">pubmed:28924239</idno><idno type="pmid">28924239</idno><idno type="doi">10.1038/s41467-017-00628-y</idno><idno type="wicri:Area/PubMed/Corpus">000586</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000586</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The autophagy initiator ULK1 sensitizes AMPK to allosteric drugs.</title><author><name sortKey="Dite, Toby A" sort="Dite, Toby A" uniqKey="Dite T" first="Toby A" last="Dite">Toby A. Dite</name><affiliation><nlm:affiliation>Metabolic Signalling Laboratory, St Vincent's Institute of Medical Research, University of Melbourne, Melbourne, VIC, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Ling, Naomi X Y" sort="Ling, Naomi X Y" uniqKey="Ling N" first="Naomi X Y" last="Ling">Naomi X Y. Ling</name><affiliation><nlm:affiliation>Metabolic Signalling Laboratory, St Vincent's Institute of Medical Research, University of Melbourne, Melbourne, VIC, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Scott, John W" sort="Scott, John W" uniqKey="Scott J" first="John W" last="Scott">John W. Scott</name><affiliation><nlm:affiliation>Protein Chemistry & Metabolism, St Vincent's Institute of Medical Research, University of Melbourne, Melbourne, VIC, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Hoque, Ashfaqul" sort="Hoque, Ashfaqul" uniqKey="Hoque A" first="Ashfaqul" last="Hoque">Ashfaqul Hoque</name><affiliation><nlm:affiliation>Metabolic Signalling Laboratory, St Vincent's Institute of Medical Research, University of Melbourne, Melbourne, VIC, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Galic, Sandra" sort="Galic, Sandra" uniqKey="Galic S" first="Sandra" last="Galic">Sandra Galic</name><affiliation><nlm:affiliation>Protein Chemistry & Metabolism, St Vincent's Institute of Medical Research, University of Melbourne, Melbourne, VIC, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Parker, Benjamin L" sort="Parker, Benjamin L" uniqKey="Parker B" first="Benjamin L" last="Parker">Benjamin L. Parker</name><affiliation><nlm:affiliation>Charles Perkins Centre, School of Molecular Bioscience, The University of Sydney, Sydney, NSW, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Ngoei, Kevin R W" sort="Ngoei, Kevin R W" uniqKey="Ngoei K" first="Kevin R W" last="Ngoei">Kevin R W. Ngoei</name><affiliation><nlm:affiliation>Protein Chemistry & Metabolism, St Vincent's Institute of Medical Research, University of Melbourne, Melbourne, VIC, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Langendorf, Christopher G" sort="Langendorf, Christopher G" uniqKey="Langendorf C" first="Christopher G" last="Langendorf">Christopher G. Langendorf</name><affiliation><nlm:affiliation>Protein Chemistry & Metabolism, St Vincent's Institute of Medical Research, University of Melbourne, Melbourne, VIC, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="O Brien, Matthew T" sort="O Brien, Matthew T" uniqKey="O Brien M" first="Matthew T" last="O'Brien">Matthew T. O'Brien</name><affiliation><nlm:affiliation>Protein Chemistry & Metabolism, St Vincent's Institute of Medical Research, University of Melbourne, Melbourne, VIC, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Kundu, Mondira" sort="Kundu, Mondira" uniqKey="Kundu M" first="Mondira" last="Kundu">Mondira Kundu</name><affiliation><nlm:affiliation>Department of Pathology, St Jude Children's Research Hospital, Memphis, TN, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Viollet, Benoit" sort="Viollet, Benoit" uniqKey="Viollet B" first="Benoit" last="Viollet">Benoit Viollet</name><affiliation><nlm:affiliation>INSERM, U1016, Institut Cochin, Paris, France.</nlm:affiliation></affiliation></author><author><name sortKey="Steinberg, Gregory R" sort="Steinberg, Gregory R" uniqKey="Steinberg G" first="Gregory R" last="Steinberg">Gregory R. Steinberg</name><affiliation><nlm:affiliation>Divisions of Endocrinology and Metabolism, Department of Medicine, and Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, ON, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Sakamoto, Kei" sort="Sakamoto, Kei" uniqKey="Sakamoto K" first="Kei" last="Sakamoto">Kei Sakamoto</name><affiliation><nlm:affiliation>MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Scotland, UK.</nlm:affiliation></affiliation></author><author><name sortKey="Kemp, Bruce E" sort="Kemp, Bruce E" uniqKey="Kemp B" first="Bruce E" last="Kemp">Bruce E. Kemp</name><affiliation><nlm:affiliation>Protein Chemistry & Metabolism, St Vincent's Institute of Medical Research, University of Melbourne, Melbourne, VIC, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Oakhill, Jonathan S" sort="Oakhill, Jonathan S" uniqKey="Oakhill J" first="Jonathan S" last="Oakhill">Jonathan S. Oakhill</name><affiliation><nlm:affiliation>Metabolic Signalling Laboratory, St Vincent's Institute of Medical Research, University of Melbourne, Melbourne, VIC, Australia. joakhill@svi.edu.au.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Nature communications</title><idno type="eISSN">2041-1723</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">AMP-activated protein kinase (AMPK) is a metabolic stress-sensing enzyme responsible for maintaining cellular energy homeostasis. Activation of AMPK by salicylate and the thienopyridone A-769662 is critically dependent on phosphorylation of Ser108 in the β1 regulatory subunit. Here, we show a possible role for Ser108 phosphorylation in cell cycle regulation and promotion of pro-survival pathways in response to energy stress. We identify the autophagy initiator Unc-51-like kinase 1 (ULK1) as a β1-Ser108 kinase in cells. Cellular β1-Ser108 phosphorylation by ULK1 was dependent on AMPK β-subunit myristoylation, metabolic stress associated with elevated AMP/ATP ratio, and the intrinsic energy sensing capacity of AMPK; features consistent with an AMP-induced myristoyl switch mechanism. We further demonstrate cellular AMPK signaling independent of activation loop Thr172 phosphorylation, providing potential insight into physiological roles for Ser108 phosphorylation. These findings uncover new mechanisms by which AMPK could potentially maintain cellular energy homeostasis independently of Thr172 phosphorylation.AMPK is involved in sensing of metabolic stress. The authors show that the autophagy initiator ULK1 phosphorylates β1-Ser108 on the regulatory β1-subunit, sensitizing AMPK to allosteric drugs, and activates signaling pathways that appear independent of Thr172 phosphorylation in the kinase activation loop.</div></front></TEI><pubmed><MedlineCitation Status="In-Data-Review" Owner="NLM"><PMID Version="1">28924239</PMID><DateCreated><Year>2017</Year><Month>09</Month><Day>19</Day></DateCreated><DateRevised><Year>2017</Year><Month>09</Month><Day>24</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2041-1723</ISSN><JournalIssue CitedMedium="Internet"><Volume>8</Volume><Issue>1</Issue><PubDate><Year>2017</Year><Month>Sep</Month><Day>18</Day></PubDate></JournalIssue><Title>Nature communications</Title><ISOAbbreviation>Nat Commun</ISOAbbreviation></Journal><ArticleTitle>The autophagy initiator ULK1 sensitizes AMPK to allosteric drugs.</ArticleTitle><Pagination><MedlinePgn>571</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/s41467-017-00628-y</ELocationID><Abstract><AbstractText>AMP-activated protein kinase (AMPK) is a metabolic stress-sensing enzyme responsible for maintaining cellular energy homeostasis. Activation of AMPK by salicylate and the thienopyridone A-769662 is critically dependent on phosphorylation of Ser108 in the β1 regulatory subunit. Here, we show a possible role for Ser108 phosphorylation in cell cycle regulation and promotion of pro-survival pathways in response to energy stress. We identify the autophagy initiator Unc-51-like kinase 1 (ULK1) as a β1-Ser108 kinase in cells. Cellular β1-Ser108 phosphorylation by ULK1 was dependent on AMPK β-subunit myristoylation, metabolic stress associated with elevated AMP/ATP ratio, and the intrinsic energy sensing capacity of AMPK; features consistent with an AMP-induced myristoyl switch mechanism. We further demonstrate cellular AMPK signaling independent of activation loop Thr172 phosphorylation, providing potential insight into physiological roles for Ser108 phosphorylation. These findings uncover new mechanisms by which AMPK could potentially maintain cellular energy homeostasis independently of Thr172 phosphorylation.AMPK is involved in sensing of metabolic stress. The authors show that the autophagy initiator ULK1 phosphorylates β1-Ser108 on the regulatory β1-subunit, sensitizing AMPK to allosteric drugs, and activates signaling pathways that appear independent of Thr172 phosphorylation in the kinase activation loop.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Dite</LastName><ForeName>Toby A</ForeName><Initials>TA</Initials><AffiliationInfo><Affiliation>Metabolic Signalling Laboratory, St Vincent's Institute of Medical Research, University of Melbourne, Melbourne, VIC, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ling</LastName><ForeName>Naomi X Y</ForeName><Initials>NXY</Initials><AffiliationInfo><Affiliation>Metabolic Signalling Laboratory, St Vincent's Institute of Medical Research, University of Melbourne, Melbourne, VIC, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Scott</LastName><ForeName>John W</ForeName><Initials>JW</Initials><AffiliationInfo><Affiliation>Protein Chemistry & Metabolism, St Vincent's Institute of Medical Research, University of Melbourne, Melbourne, VIC, Australia.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Mary MacKillop Institute for Health Research, Australian Catholic University, Melbourne, VIC, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hoque</LastName><ForeName>Ashfaqul</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Metabolic Signalling Laboratory, St Vincent's Institute of Medical Research, University of Melbourne, Melbourne, VIC, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Galic</LastName><ForeName>Sandra</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Protein Chemistry & Metabolism, St Vincent's Institute of Medical Research, University of Melbourne, Melbourne, VIC, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Parker</LastName><ForeName>Benjamin L</ForeName><Initials>BL</Initials><AffiliationInfo><Affiliation>Charles Perkins Centre, School of Molecular Bioscience, The University of Sydney, Sydney, NSW, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ngoei</LastName><ForeName>Kevin R W</ForeName><Initials>KRW</Initials><AffiliationInfo><Affiliation>Protein Chemistry & Metabolism, St Vincent's Institute of Medical Research, University of Melbourne, Melbourne, VIC, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Langendorf</LastName><ForeName>Christopher G</ForeName><Initials>CG</Initials><AffiliationInfo><Affiliation>Protein Chemistry & Metabolism, St Vincent's Institute of Medical Research, University of Melbourne, Melbourne, VIC, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>O'Brien</LastName><ForeName>Matthew T</ForeName><Initials>MT</Initials><AffiliationInfo><Affiliation>Protein Chemistry & Metabolism, St Vincent's Institute of Medical Research, University of Melbourne, Melbourne, VIC, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kundu</LastName><ForeName>Mondira</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Pathology, St Jude Children's Research Hospital, Memphis, TN, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Viollet</LastName><ForeName>Benoit</ForeName><Initials>B</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-0121-0224</Identifier><AffiliationInfo><Affiliation>INSERM, U1016, Institut Cochin, Paris, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>CNRS, UMR8104, Paris, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Université Paris Descartes, Sorbonne Paris Cité, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Steinberg</LastName><ForeName>Gregory R</ForeName><Initials>GR</Initials><AffiliationInfo><Affiliation>Divisions of Endocrinology and Metabolism, Department of Medicine, and Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, ON, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sakamoto</LastName><ForeName>Kei</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Scotland, UK.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Nestlé Institute of Health Sciences SA, Lausanne, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kemp</LastName><ForeName>Bruce E</ForeName><Initials>BE</Initials><Identifier Source="ORCID">http://orcid.org/0000-0001-6735-5082</Identifier><AffiliationInfo><Affiliation>Protein Chemistry & Metabolism, St Vincent's Institute of Medical Research, University of Melbourne, Melbourne, VIC, Australia.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Mary MacKillop Institute for Health Research, Australian Catholic University, Melbourne, VIC, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Oakhill</LastName><ForeName>Jonathan S</ForeName><Initials>JS</Initials><AffiliationInfo><Affiliation>Metabolic Signalling Laboratory, St Vincent's Institute of Medical Research, University of Melbourne, Melbourne, VIC, Australia. joakhill@svi.edu.au.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Mary MacKillop Institute for Health Research, Australian Catholic University, Melbourne, VIC, Australia. joakhill@svi.edu.au.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate 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