Function and regulation of ubiquitin-like SUMO system in heart

Front Cell Dev Biol. 2023 Nov 16:11:1294717. doi: 10.3389/fcell.2023.1294717. eCollection 2023.

Abstract

The small ubiquitin-related modifier (SUMOylation) system is a conserved, reversible, post-translational protein modification pathway covalently attached to the lysine residues of proteins in eukaryotic cells, and SUMOylation is catalyzed by SUMO-specific activating enzyme (E1), binding enzyme (E2) and ligase (E3). Sentrin-specific proteases (SENPs) can cleave the isopeptide bond of a SUMO conjugate and catalyze the deSUMOylation reaction. SUMOylation can regulate the activity of proteins in many important cellular processes, including transcriptional regulation, cell cycle progression, signal transduction, DNA damage repair and protein stability. Biological experiments in vivo and in vitro have confirmed the key role of the SUMO conjugation/deconjugation system in energy metabolism, Ca2+ cycle homeostasis and protein quality control in cardiomyocytes. In this review, we summarized the research progress of the SUMO conjugation/deconjugation system and SUMOylation-mediated cardiac actions based on related studies published in recent years, and highlighted the further research areas to clarify the role of the SUMO system in the heart by using emerging technologies.

Keywords: Ca2+ cycle; SUMO; cardiac metabolism; heart; protein quality control.

Publication types

  • Review

Grants and funding

The author(s) declare financial support was received for the research, authorship, and/or publication of this article. This research was funded by The National Natural Science Foundation of China (No. U20A20400), and The National Natural Science Foundation of China Number (No. 82270304), and The Innovative Research Team of Tianjin Municipal Education Commission Number (No. TD13-5015), and The Jinan Innovation Team Project (No. 202228040).