PXD011473-1

PXD011473 is an original dataset announced via ProteomeXchange.

Title	Understanding the physiological role of asparaginyl endopeptidase (AEP)/Legumain
Description	Understanding 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.
HostingRepository	PRIDE
AnnounceDate	2019-01-09
AnnouncementXML	Submission_2019-01-09_04:14:05.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Jonathan Martinez Fabregas
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	6x(13)C labeled residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2018-10-25 03:39:21	ID requested
⏵ 1	2019-01-09 04:14:07	announced

Mart, í, nez-F, á, bregas 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]

submitter keyword: WT MEFs, MVO26630, time course, nanoLC-MS/MS

Colin Watts
contact affiliation	Cell Signaling and Immunology, School of Life Science, University of Dundee, Dundee. United Kingdom
contact email	c.watts@dundee.ac.uk
lab head
Jonathan Martinez Fabregas
contact affiliation	Cell Signaling and Immunology
contact email	jmartinezfabregas@dundee.ac.uk
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/01/PXD011473

PRIDE project URI

• PRIDE
  1. PXD011473
     1. Label: PRIDE project
     2. Name: Understanding the physiological role of asparaginyl endopeptidase (AEP)/Legumain