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PXD011473

PXD011473 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleUnderstanding the physiological role of asparaginyl endopeptidase (AEP)/Legumain
DescriptionUnderstanding the regulation of lysosomal proteolytic/hidrolytic capacity has been recently advanced in a huge manner by the discovery of the lysosome-mTOR-TFEB pathway connecting nutrient sensing, autophagy and de novo lysosome generation. But, how lysosomes can adjust their proteolytic/hidrolytic capacity to meet varying conditions (more or less substrate) under normal fed conditions is not known. We have used AEP as a proxy to understand how lysosomes can compensate the lack of a key lysosomal protease to meet the requirements under physiological, fed conditions. To do this, we did compare cytoplasmic, membrane and nuclear fractions of WT and AEP MEFs that were expanded in SILAC media. AEP knock-out mice show pale kidney, with abnormal proliferation of the epithelial proximal tubular cells. In an attempt to understand the role of AEP in the kidney, we did compare kidney obtained from WT and AEP mice using kidneys from WT mice that were fed with SILAC food. Also, in an attempt to reproduce the changes observed in the absence of AEP in kidney and MEFs, we treated WT MEFs grown in SILAC media with MVO26630, specific inhibitor of AEP, for 12 and 48 hours.
HostingRepositoryPRIDE
AnnounceDate2019-01-09
AnnouncementXMLSubmission_2019-01-09_04:14:05.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterJonathan Martinez Fabregas
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList6x(13)C labeled residue; monohydroxylated residue; iodoacetamide derivatized residue
InstrumentLTQ Orbitrap Velos
Dataset History
RevisionDatetimeStatusChangeLog Entry
02018-10-25 03:39:21ID requested
12019-01-09 04:14:07announced
Publication List
Martínez-Fábregas J, Prescott A, van Kasteren S, Pedrioli DL, McLean I, Moles A, Reinheckel T, Poli V, Watts C, Lysosomal protease deficiency or substrate overload induces an oxidative-stress mediated STAT3-dependent pathway of lysosomal homeostasis. Nat Commun, 9(1):5343(2018) [pubmed]
Keyword List
submitter keyword: WT MEFs, MVO26630, time course, nanoLC-MS/MS
Contact List
Colin Watts
contact affiliationCell Signaling and Immunology, School of Life Science, University of Dundee, Dundee. United Kingdom
contact emailc.watts@dundee.ac.uk
lab head
Jonathan Martinez Fabregas
contact affiliationCell Signaling and Immunology
contact emailjmartinezfabregas@dundee.ac.uk
dataset submitter
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Dataset FTP location
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