Protein Lysine Acylation: Abundance, Dynamics and Function

Olga Pougovkina, Vincent de Boer

    Research output: Chapter in Book/Report/Conference proceedingChapterAcademicpeer-review

    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.
    Original languageEnglish
    Title of host publicationSirtuins
    EditorsRiekelt H. Houtkooper
    Place of PublicationDordrecht
    PublisherSpringer
    Chapter3
    Pages41-69
    ISBN (Electronic)9789402409628
    ISBN (Print)9789402409611
    DOIs
    Publication statusPublished - 18 Nov 2016

    Publication series

    NameProteins and Cell Regulation
    Volume10
    ISSN (Print)1567-2530
    ISSN (Electronic)2542-9973

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