In-Depth Characterization of Apoptosis N-Terminome Reveals a Link Between Caspase-3 Cleavage and Posttranslational N-Terminal Acetylation.

Autor:	Hanna R; Faculty of Biology, Technion-Israel Institute of Technology, Haifa, Israel., Rozenberg A; Faculty of Biology, Technion-Israel Institute of Technology, Haifa, Israel., Saied L; Faculty of Biology, Technion-Israel Institute of Technology, Haifa, Israel., Ben-Yosef D; Faculty of Biology, Technion-Israel Institute of Technology, Haifa, Israel., Lavy T; Faculty of Biology, Technion-Israel Institute of Technology, Haifa, Israel., Kleifeld O; Faculty of Biology, Technion-Israel Institute of Technology, Haifa, Israel. Electronic address: okleifeld@technion.ac.il.
Jazyk:	angličtina
Zdroj:	Molecular & cellular proteomics : MCP [Mol Cell Proteomics] 2023 Jul; Vol. 22 (7), pp. 100584. Date of Electronic Publication: 2023 May 24.
DOI:	10.1016/j.mcpro.2023.100584
Abstrakt:	The N termini of proteins contain information about their biochemical properties and functions. These N termini can be processed by proteases and can undergo other co- or posttranslational modifications. We have developed LATE (LysN Amino Terminal Enrichment), a method that uses selective chemical derivatization of α-amines to isolate the N-terminal peptides, in order to improve N-terminome identification in conjunction with other enrichment strategies. We applied LATE alongside another N-terminomic method to study caspase-3-mediated proteolysis both in vitro and during apoptosis in cells. This has enabled us to identify many unreported caspase-3 cleavages, some of which cannot be identified by other methods. Moreover, we have found direct evidence that neo-N-termini generated by caspase-3 cleavage can be further modified by Nt-acetylation. Some of these neo-Nt-acetylation events occur in the early phase of the apoptotic process and may have a role in translation inhibition. This has provided a comprehensive overview of the caspase-3 degradome and has uncovered previously unrecognized cross talk between posttranslational Nt-acetylation and caspase proteolytic pathways. Competing Interests: Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article. (Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.)
Databáze:	MEDLINE
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