Proteomics

Dataset Information

0

Tracking Proteasome Degradation: A Cross-Organ Analysis via Intact degradomics Top-Down Mass Spectrometry


ABSTRACT: Identifying the peptides generated by the proteasome is essential for understanding its role in regulating critical cellular processes such as apoptosis, signaling, and immune responses. In this study, we introduce an enzymatic top-down mass spectrometry approach that allows real-time monitoring of proteasome-mediated cleavage, providing detailed insights into substrate degradation patterns. By examining proteasomes from different organs, we reveal organ-specific peptide production and degradation behaviors, offering a deeper understanding of how proteasome subtypes affect cellular function. This method is well-suited for investigating the influence of proteasome regulators, inhibitors and activators, on proteasome activity. Additionally, its versatility makes it applicable to other proteolytic complexes, paving the way for further research on proteostasis systems.

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Spleen, Brain, Liver

SUBMITTER: Katharina Zittlau  

LAB HEAD: Michal Sharon

PROVIDER: PXD058121 | Pride | 2025-08-25

REPOSITORIES: Pride

Dataset's files

Source:
altmetric image

Publications

Tracking proteasome degradation: A cross-organ analysis via intact degradomics mass spectrometry.

Zittlau Katharina I KI   Zachor-Movshovitz Daniel D   Leushkin Yegor Y   Schimmel Brener Roy R   Morgenstern David D   Ben-Nissan Gili G   Sharon Michal M  

Proceedings of the National Academy of Sciences of the United States of America 20250218 8


The proteasome is a multisubunit degradation machinery that is essential for maintaining protein homeostasis by breaking down unnecessary or damaged proteins into peptides. While most of these peptides are further processed into amino acids, a subset evades complete degradation and plays key roles in biological processes such as antigen presentation, signaling, and apoptosis. However, the variability in peptide lengths and the diverse composition of proteasomes make their comprehensive identific  ...[more]

Similar Datasets

2015-02-09 | PXD001462 | Pride
2023-06-27 | PXD039993 | Pride
2023-01-10 | PXD031627 | Pride
2022-02-17 | PXD027786 | Pride
2023-01-10 | PXD031616 | Pride
2007-12-20 | E-MEXP-1383 | biostudies-arrayexpress
2013-10-28 | E-GEOD-51781 | biostudies-arrayexpress
2023-04-07 | PXD027349 | Pride
2022-02-22 | PXD028830 | Pride
2015-11-04 | E-GEOD-74633 | biostudies-arrayexpress