The growing landscape of lysine acetylation links metabolism and cell signalling

Research output: Contribution to journal › Review › Research › peer-review

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The growing landscape of lysine acetylation links metabolism and cell signalling. / Choudhary, Chuna Ram; Weinert, Brian Tate; Nishida, Yuya; Verdin, Eric; Mann, Matthias.

In: Nature Reviews. Molecular Cell Biology, Vol. 15, No. 8, 23.07.2014, p. 536-50.

Research output: Contribution to journal › Review › Research › peer-review

Harvard

Choudhary, CR, Weinert, BT, Nishida, Y, Verdin, E & Mann, M 2014, 'The growing landscape of lysine acetylation links metabolism and cell signalling', Nature Reviews. Molecular Cell Biology, vol. 15, no. 8, pp. 536-50. https://doi.org/10.1038/nrm3841

APA

Choudhary, C. R., Weinert, B. T., Nishida, Y., Verdin, E., & Mann, M. (2014). The growing landscape of lysine acetylation links metabolism and cell signalling. Nature Reviews. Molecular Cell Biology, 15(8), 536-50. https://doi.org/10.1038/nrm3841

Vancouver

Choudhary CR, Weinert BT, Nishida Y, Verdin E, Mann M. The growing landscape of lysine acetylation links metabolism and cell signalling. Nature Reviews. Molecular Cell Biology. 2014 Jul 23;15(8):536-50. https://doi.org/10.1038/nrm3841

Author

Choudhary, Chuna Ram ; Weinert, Brian Tate ; Nishida, Yuya ; Verdin, Eric ; Mann, Matthias. / The growing landscape of lysine acetylation links metabolism and cell signalling. In: Nature Reviews. Molecular Cell Biology. 2014 ; Vol. 15, No. 8. pp. 536-50.

Bibtex

@article{22c98317f15f40b886f6d81101421a94,
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",
year = "2014",
month = jul,
day = "23",
doi = "10.1038/nrm3841",
language = "English",
volume = "15",
pages = "536--50",
journal = "Nature Reviews. Molecular Cell Biology",
issn = "1471-0072",
publisher = "nature publishing group",
number = "8",

}

RIS

TY - JOUR

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 - 2014/7/23

Y1 - 2014/7/23

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.

U2 - 10.1038/nrm3841

DO - 10.1038/nrm3841

M3 - Review

C2 - 25053359

VL - 15

SP - 536

EP - 550

JO - Nature Reviews. Molecular Cell Biology

JF - Nature Reviews. Molecular Cell Biology

SN - 1471-0072

IS - 8

ER -

ID: 122429977