PXD036593

PXD036593 is an original dataset announced via ProteomeXchange.

Title	In vitro characterization of caspase-3 cleavage sites by LATE and HYATNE
Description	Proteins' N-termini contain information about their biochemical properties and functions, and they can undergo co- or post-translational modifications, as well as be processed by proteases. To expand the coverage of the N-terminome, we have developed LATE (LysN Amino Terminal Enrichment), a method that uses selective chemical derivatization of α-amines to isolate the N-terminal peptides. We applied LATE in combination with other N-terminomic method to study caspase-3 mediated proteolysis both in vitro and during apoptosis in cells. This enable us to identify many unreported caspase-3 cleavages, including some that cannot be identified by other methods. Furthermore, we find direct evidence that some of the caspase-3 generated neo-N-termini can be further modified by Nt-acetylation. This provides a global picture of the caspase-3 degradome and uncovers previously unrecognised functional crosstalk between post-translational Nt-acetylation and caspase proteolysis pathways.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_05:50:53.997.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Oded Kleifeld
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monomethylated residue; acetylated residue; alpha-amino dimethylated residue; iodoacetamide derivatized residue; N6,N6-dimethyl-L-lysine
Instrument	Q Exactive HF; Q Exactive Plus

Revision	Datetime	Status	ChangeLog Entry
0	2022-09-08 07:50:42	ID requested
1	2024-10-07 13:47:27	announced
⏵ 2	2024-10-22 05:50:54	announced	2024-10-22: Updated project metadata.

10.1016/j.mcpro.2023.100584;

Hanna R, Rozenberg A, Saied L, Ben-Yosef D, Lavy T, Kleifeld O, In-Depth Characterization of Apoptosis N-Terminome Reveals a Link Between Caspase-3 Cleavage and Posttranslational N-Terminal Acetylation. Mol Cell Proteomics, 22(7):100584(2023) [pubmed]

submitter keyword: LATE, HYTANE,LysN, Peptidyl-Lys metalloendopeptidase N-terminomics, Caspase-3

Oded Kleifeld
contact affiliation	Faculty of Biology, Technion - Israel Institute of Technology Haifa, Israel
contact email	okleifeld@technion.ac.il
lab head
Oded Kleifeld
contact affiliation	Technion
contact email	okleifeld@technion.ac.il
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/2023/06/PXD036593

PRIDE project URI

• PRIDE
  1. PXD036593
     1. Label: PRIDE project
     2. Name: In vitro characterization of caspase-3 cleavage sites by LATE and HYATNE