PXD048603

PXD048603 is an original dataset announced via ProteomeXchange.

Title	Cellular Depletion of Major Cathepsin Proteases in HeLa and SH-SY5Y Cells
Description	Proteins delivered by endocytosis or autophagy to lysosomes are degraded by exo- and endoproteases. In humans there are 15 lysosomal cathepsins (CTS) that act as important physiological regulators. The cysteine proteases CTSB and CTSL and the aspartic protease CTSD are the most abundant lysosomal proteinases and are often linked to autophagy, lysosomal storage and neurodegenerative diseases. Their concerted functions in proteolysis in the lysosome, their individual substrates, cleavage specificity, functional redundancy, and possible sequential action on substrate proteins are not well understood. To address these open points, we generated CTSB-, CTSD-, CTSL-, and CTSBDL-triple deficient (KO) human neuroblastoma-derived SH-SY5Y cells and CTSB-, CTSD-, CTSL-, CTSZ and CTSBDLZ-quadruple deficient (KO) HeLa cells. Proteome analyses of parental and CTS-depleted cells revealed an enrichment of semitryptic peptides and of lysosome/autophagy-associated proteins but also of potentially endocytosed membrane proteins like the amyloid precursor protein (APP). Amino- and carboxyterminal APP fragments accumulated in the multiple CTS-deficient cells, suggesting that APP is regularly processed by multiple CTS-mediated cleavage events.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_06:42:55.887.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Stephan Mueller
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2024-01-16 06:49:01	ID requested
1	2024-05-24 09:04:23	announced
⏵ 2	2024-10-22 06:42:56	announced	2024-10-22: Updated project metadata.

10.1007/s00018-024-05274-4;

Gallwitz L, Bleibaum F, Voss M, Schweizer M, Spengler K, Winter D, Z, ö, phel F, M, ü, ller S, Lichtenthaler S, Damme M, Saftig P, Cellular depletion of major cathepsin proteases reveals their concerted activities for lysosomal proteolysis. Cell Mol Life Sci, 81(1):227(2024) [pubmed]

submitter keyword: Cathepsin, lysosome, HeLa, SH-SY5Y, proteolysis

Stefan F. Lichtenthaler
contact affiliation	DZNE Munich, Neuroproteomics, Feodor-Lynen Str. 17, 81377 Munich, Germany
contact email	stefan.lichetnthaler@dzne.de
lab head
Stephan Mueller
contact affiliation	DZNE Munich Neuroproteomics
contact email	stephan.mueller@dzne.de
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/2024/05/PXD048603

PRIDE project URI

• PRIDE
  1. PXD048603
     1. Label: PRIDE project
     2. Name: Cellular Depletion of Major Cathepsin Proteases in HeLa and SH-SY5Y Cells