PXD001245

PXD001245 is an original dataset announced via ProteomeXchange.

Title	Functional proteomics identifies acinus L as a direct insulin- and amino acid-dependent mTORC1 substrate
Description	The serine/threonine kinase mammalian target of rapamycin (mTOR) governs growth, metabolism, and aging in response to insulin and amino acids (aa), and is often activated in metabolic disorders and cancer. Much is known about the regulatory signaling network around mTOR, but surprisingly few direct mTOR substrates have been established to date. To tackle this gap in our knowledge, we took advantage of a combined quantitative phosphoproteomic and interactomic strategy. We analyzed the insulin- and aa-responsive phosphoproteome upon inhibition of the mTOR complex 1 (mTORC1) component raptor, and analyzed in parallel the interactome of endogenous mTOR. By overlaying these two datasets, we identified acinus L as a potential novel mTORC1 target. We confirmed acinus L as a direct mTORC1 substrate by co-immunoprecipitation and MS-enhanced kinase assays. Our study delineates a triple proteomics strategy of combined phosphoproteomics, interactomics, and MS-enhanced kinase assays for the de novo-identification of mTOR network components, and provides a rich source of potential novel mTOR interactors and targets for future investigation. Additional contact details: Prof. Dr. Kathrin Thedieck Department of Pediatrics, University of Groningen, University Medical Center Groningen (UMCG), 9713 AV Groningen, The Netherlands. Faculty VI - School of Medicine and Health Sciences, Carl von Ossietzky University Oldenburg, 26111 Oldenburg, Germany. Prof. Dr. Bettina Warscheid Faculty of Biology, Institute of Biology II, University of Freiburg, 79104 Freiburg, Germany. BIOSS Centre for Biological Signalling Studies, University of Freiburg, 79104 Freiburg, Germany.
HostingRepository	PRIDE
AnnounceDate	2015-04-28
AnnouncementXML	Submission_2015-04-28_04:54:30.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Friedel Drepper
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue; phosphorylated residue
Instrument	LTQ Orbitrap; LTQ FT

Revision	Datetime	Status	ChangeLog Entry
0	2014-08-18 02:28:27	ID requested
⏵ 1	2015-04-28 04:54:31	announced

Schwarz JJ, Wiese H, T, ö, lle RC, Zarei M, Dengjel J, Warscheid B, Thedieck K, Functional Proteomics Identifies Acinus L as a Direct Insulin- and Amino Acid-Dependent Mammalian Target of Rapamycin Complex 1 (mTORC1) Substrate. Mol Cell Proteomics, 14(8):2042-55(2015) [pubmed]

curator keyword: Biomedical

submitter keyword: human, mTOR, LC-MS, MS-based in vitro kinase assay

Prof. Dr. Kathrin Thedieck
contact affiliation	Department of Pediatrics, University of Groningen, University Medical Center Groningen (UMCG), 9713 AV Groningen, The Netherlands
contact email	k.thedieck@umcg.nl
lab head
Friedel Drepper
contact affiliation	AG Warscheid Biologie II Albert-Ludwigs-Universität Freiburg Schänzlestr. 1 79104 Freiburg Germany
contact email	friedel.drepper@biologie.uni-freiburg.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD001245
     1. Label: PRIDE project
     2. Name: Functional proteomics identifies acinus L as a direct insulin- and amino acid-dependent mTORC1 substrate