PXD006365 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Quantitative global and phosphoproteomic analysis to define the cellular role of AMPK β1-Ser108 phosphorylation |
Description | 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. We identified the autophagy initiator Unc-51-like kinase 1 (ULK1) as a β1-Ser108 kinase. ULK1 phosphorylation was specific to the β1-isoform and sensitised AMPK to salicylate and A-769662. To investigate the cellular fate of β1-Ser108 phosphorylation, we performed a stable isotope dimethyl labelling-based quantitative proteomic and phosphoproteomic analysis using lentivirus-transduced S108A and S108E mutants of β1 in β1/2-dKO iMEFs cells. Following 1 h phenformin (2 mM) treatment, β1-S108A and β1-S108E transduced iMEF lysates were compared to trace out the changes in proteome and phosphoprotome to decipher the possible cellular role of β1-Ser108 phosphorylation. |
HostingRepository | PRIDE |
AnnounceDate | 2018-10-24 |
AnnouncementXML | Submission_2018-10-24_14:00:28.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Ashfaqul Hoque |
SpeciesList | scientific name: Mus musculus (Mouse); NCBI TaxID: 10090; |
ModificationList | phosphorylated residue; dimethylated residue; iodoacetamide derivatized residue |
Instrument | Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2017-04-24 06:07:52 | ID requested | |
⏵ 1 | 2018-10-24 14:00:30 | announced | |
Publication List
Dite TA, Ling NXY, Scott JW, Hoque A, Galic S, Parker BL, Ngoei KRW, Langendorf CG, O'Brien MT, Kundu M, Viollet B, Steinberg GR, Sakamoto K, Kemp BE, Oakhill JS, The autophagy initiator ULK1 sensitizes AMPK to allosteric drugs. Nat Commun, 8(1):571(2017) [pubmed] |
Keyword List
curator keyword: Biological |
submitter keyword: AMPK β1-Ser108, ULK1, autophagy |
Contact List
Jonathan S. Oakhill |
contact affiliation | ARC Future Fellow Head, Metabolic Signalling Laboratory Protein Chemistry and Metabolism St. Vincent's Institute of Medical Research 9 Princes St, Fitzroy, Vic 3065, Australia |
contact email | joakhill@svi.edu.au |
lab head | |
Ashfaqul Hoque |
contact affiliation | St Vincent's Institute of Medical Research (SVI) |
contact email | ahoque@svi.edu.au |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
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- PRIDE
- PXD006365
- Label: PRIDE project
- Name: Quantitative global and phosphoproteomic analysis to define the cellular role of AMPK β1-Ser108 phosphorylation