The growing landscape of lysine acetylation links metabolism and cell signalling

Chuna Ram Choudhary; Brian Tate Weinert; Yuya Nishida; Eric Verdin; Matthias Mann

doi:10.1038/nrm3841

The growing landscape of lysine acetylation links metabolism and cell signalling

Chuna Ram Choudhary, Brian Tate Weinert, Yuya Nishida, Eric Verdin, Matthias Mann

Novo Nordisk Foundation Center for Protein Research

725 Citations (Scopus)

Abstract

Lysine acetylation is a conserved protein post-translational modification that links acetyl-coenzyme A metabolism and cellular signalling. Recent advances in the identification and quantification of lysine acetylation by mass spectrometry have increased our understanding of lysine acetylation, implicating it in many biological processes through the regulation of protein interactions, activity and localization. In addition, proteins are frequently modified by other types of acylations, such as formylation, butyrylation, propionylation, succinylation, malonylation, myristoylation, glutarylation and crotonylation. The intricate link between lysine acylation and cellular metabolism has been clarified by the occurrence of several such metabolite-sensitive acylations and their selective removal by sirtuin deacylases. These emerging findings point to new functions for different lysine acylations and deacylating enzymes and also highlight the mechanisms by which acetylation regulates various cellular processes.

Original language	English
Journal	Nature Reviews. Molecular Cell Biology
Volume	15
Issue number	8
Pages (from-to)	536-50
Number of pages	15
ISSN	1471-0072
DOIs	https://doi.org/10.1038/nrm3841
Publication status	Published - Aug 2014

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title = "The growing landscape of lysine acetylation links metabolism and cell signalling",

abstract = "Lysine acetylation is a conserved protein post-translational modification that links acetyl-coenzyme A metabolism and cellular signalling. Recent advances in the identification and quantification of lysine acetylation by mass spectrometry have increased our understanding of lysine acetylation, implicating it in many biological processes through the regulation of protein interactions, activity and localization. In addition, proteins are frequently modified by other types of acylations, such as formylation, butyrylation, propionylation, succinylation, malonylation, myristoylation, glutarylation and crotonylation. The intricate link between lysine acylation and cellular metabolism has been clarified by the occurrence of several such metabolite-sensitive acylations and their selective removal by sirtuin deacylases. These emerging findings point to new functions for different lysine acylations and deacylating enzymes and also highlight the mechanisms by which acetylation regulates various cellular processes.",

author = "Choudhary, {Chuna Ram} and Weinert, {Brian Tate} and Yuya Nishida and Eric Verdin and Matthias Mann",

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T1 - The growing landscape of lysine acetylation links metabolism and cell signalling

AU - Choudhary, Chuna Ram

AU - Weinert, Brian Tate

AU - Nishida, Yuya

AU - Verdin, Eric

AU - Mann, Matthias

PY - 2014/8

Y1 - 2014/8

N2 - Lysine acetylation is a conserved protein post-translational modification that links acetyl-coenzyme A metabolism and cellular signalling. Recent advances in the identification and quantification of lysine acetylation by mass spectrometry have increased our understanding of lysine acetylation, implicating it in many biological processes through the regulation of protein interactions, activity and localization. In addition, proteins are frequently modified by other types of acylations, such as formylation, butyrylation, propionylation, succinylation, malonylation, myristoylation, glutarylation and crotonylation. The intricate link between lysine acylation and cellular metabolism has been clarified by the occurrence of several such metabolite-sensitive acylations and their selective removal by sirtuin deacylases. These emerging findings point to new functions for different lysine acylations and deacylating enzymes and also highlight the mechanisms by which acetylation regulates various cellular processes.

AB - Lysine acetylation is a conserved protein post-translational modification that links acetyl-coenzyme A metabolism and cellular signalling. Recent advances in the identification and quantification of lysine acetylation by mass spectrometry have increased our understanding of lysine acetylation, implicating it in many biological processes through the regulation of protein interactions, activity and localization. In addition, proteins are frequently modified by other types of acylations, such as formylation, butyrylation, propionylation, succinylation, malonylation, myristoylation, glutarylation and crotonylation. The intricate link between lysine acylation and cellular metabolism has been clarified by the occurrence of several such metabolite-sensitive acylations and their selective removal by sirtuin deacylases. These emerging findings point to new functions for different lysine acylations and deacylating enzymes and also highlight the mechanisms by which acetylation regulates various cellular processes.

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DO - 10.1038/nrm3841

M3 - Review

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SN - 1471-0072

VL - 15

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EP - 550

JO - Nature Reviews. Molecular Cell Biology

JF - Nature Reviews. Molecular Cell Biology

IS - 8

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The growing landscape of lysine acetylation links metabolism and cell signalling

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