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Protein Lysine Acylation: Abundance, Dynamics and Function

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Sirtuins

Part of the book series: Proteins and Cell Regulation ((PROR,volume 10))

Abstract

Lysine acylation comprises a group of post-translational modifications which involve the transfer of an acyl group to ε-amino group of a lysine residue. Most studied acylation modification is acetylation, however recently, a number of new acylation modifications have been discovered. These include formylation, propionylation, butyrylation, malonylation, succinylation, glutarylation and crotonylation. In this chapter, we review the discovery of various acylation modifications and the current insight into their function, regulation and dynamics.

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Authors and Affiliations

  1. Laboratory Genetic Metabolic Diseases, Department of Clinical Chemistry, Academic Medical Center, Meibergdreef 9, 1105 AZ, Amsterdam, The Netherlands

    Olga Pougovkina & Vincent C. J. de Boer

  2. Human and Animal Physiology, Wageningen University and Research, De Elst 1, 6708 WD, Wageningen, The Netherlands

    Vincent C. J. de Boer

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    Riekelt H. Houtkooper

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Pougovkina, O., de Boer, V.C.J. (2016). Protein Lysine Acylation: Abundance, Dynamics and Function. In: Houtkooper, R. (eds) Sirtuins. Proteins and Cell Regulation, vol 10. Springer, Dordrecht. https://doi.org/10.1007/978-94-024-0962-8_3

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