The autophagy initiator ULK1 sensitizes AMPK to allosteric drugs
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...
| Main Authors: | , , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2017-09-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-017-00628-y |
| _version_ | 1819041958714146816 |
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| author | 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. Oakhill |
| author_facet | 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. Oakhill |
| author_sort | Toby A. Dite |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-21T09:33:16Z |
| format | Article |
| id | doaj.art-165d7eeb69bd4fda9ad259d85d17b5a6 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-21T09:33:16Z |
| publishDate | 2017-09-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-165d7eeb69bd4fda9ad259d85d17b5a62022-12-21T19:08:41ZengNature PortfolioNature Communications2041-17232017-09-018111410.1038/s41467-017-00628-yThe autophagy initiator ULK1 sensitizes AMPK to allosteric drugsToby A. Dite0Naomi X. Y. Ling1John W. Scott2Ashfaqul Hoque3Sandra Galic4Benjamin L. Parker5Kevin R. W. Ngoei6Christopher G. Langendorf7Matthew T. O’Brien8Mondira Kundu9Benoit Viollet10Gregory R. Steinberg11Kei Sakamoto12Bruce E. Kemp13Jonathan S. Oakhill14Metabolic Signalling Laboratory, St Vincent’s Institute of Medical Research, University of MelbourneMetabolic Signalling Laboratory, St Vincent’s Institute of Medical Research, University of MelbourneProtein Chemistry & Metabolism, St Vincent’s Institute of Medical Research, University of MelbourneMetabolic Signalling Laboratory, St Vincent’s Institute of Medical Research, University of MelbourneProtein Chemistry & Metabolism, St Vincent’s Institute of Medical Research, University of MelbourneCharles Perkins Centre, School of Molecular Bioscience, The University of SydneyProtein Chemistry & Metabolism, St Vincent’s Institute of Medical Research, University of MelbourneProtein Chemistry & Metabolism, St Vincent’s Institute of Medical Research, University of MelbourneProtein Chemistry & Metabolism, St Vincent’s Institute of Medical Research, University of MelbourneDepartment of Pathology, St Jude Children’s Research HospitalINSERM, U1016, Institut CochinDivisions of Endocrinology and Metabolism, Department of Medicine, and Department of Biochemistry and Biomedical Sciences, McMaster UniversityMRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of DundeeProtein Chemistry & Metabolism, St Vincent’s Institute of Medical Research, University of MelbourneMetabolic Signalling Laboratory, St Vincent’s Institute of Medical Research, University of MelbourneAMPK 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.https://doi.org/10.1038/s41467-017-00628-y |
| spellingShingle | 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. Oakhill The autophagy initiator ULK1 sensitizes AMPK to allosteric drugs Nature Communications |
| title | The autophagy initiator ULK1 sensitizes AMPK to allosteric drugs |
| title_full | The autophagy initiator ULK1 sensitizes AMPK to allosteric drugs |
| title_fullStr | The autophagy initiator ULK1 sensitizes AMPK to allosteric drugs |
| title_full_unstemmed | The autophagy initiator ULK1 sensitizes AMPK to allosteric drugs |
| title_short | The autophagy initiator ULK1 sensitizes AMPK to allosteric drugs |
| title_sort | autophagy initiator ulk1 sensitizes ampk to allosteric drugs |
| url | https://doi.org/10.1038/s41467-017-00628-y |
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