An Expanding Repertoire of Protein Acylations.

Abstract

Protein post-translational modifications play key roles in multiple cellular processes by allowing rapid reprogramming of individual protein functions. Acylation, one of the most important post-translational modifications, is involved in different physiological activities including cell differentiation and energy metabolism. In recent years, the progression in technologies, especially the antibodies against acylation and the highly sensitive and effective mass spectrometry-based proteomics, as well as optimized functional studies, greatly deepen our understanding of protein acylation. In this review, we give a general overview of the 12 main protein acylations (formylation, acetylation, propionylation, butyrylation, malonylation, succinylation, glutarylation, palmitoylation, myristoylation, benzoylation, crotonylation, and 2-hydroxyisobutyrylation), including their substrates (histones and nonhistone proteins), regulatory enzymes (writers, readers, and erasers), biological functions (transcriptional regulation, metabolic regulation, subcellular targeting, protein-membrane interactions, protein stability, and folding), and related diseases (cancer, diabetes, heart disease, neurodegenerative disease, and viral infection), to present a complete picture of protein acylations and highlight their functional significance in future research.

• Authors: Yuxuan Xu, Zhenyu Shi, Li Bao
• Journal: Molecular & cellular proteomics : MCP (Mol Cell Proteomics) Vol. 21 Issue 3 Pg. 100193 (03 2022) ISSN: 1535-9484 [Electronic] United States
• PMID: 34999219 (Publication Type: Journal Article, Review, Research Support, Non-U.S. Gov't)
• Copyright: Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved.

Chemical References

• Histones
• Lysine

Topics

• Acetylation
• Acylation
• Histones (metabolism)
• Humans
• Lysine (metabolism)
• Neurodegenerative Diseases
• Protein Processing, Post-Translational