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Review
. 2010 Apr;67(8):1255-64.
doi: 10.1007/s00018-009-0252-7. Epub 2010 Jan 16.

The emerging role of lysine acetylation of non-nuclear proteins

Pierre Close  1 , Catherine Creppe, Magali Gillard, Aurélie Ladang, Jean-Paul Chapelle, Laurent Nguyen, Alain Chariot
Affiliations
Review

The emerging role of lysine acetylation of non-nuclear proteins

Pierre Close et al. Cell Mol Life Sci. 2010 Apr.

Abstract

Lysine acetylation is a post-translational modification that critically regulates gene transcription by targeting histones as well as a variety of transcription factors in the nucleus. More recent reports have also demonstrated that numerous proteins located outside the nucleus are also acetylated and that this modification has profound consequences on their functions. This review describes the latest findings on the substrates acetylated outside the nucleus and on the acetylases and deacetylates that catalyse these modifications. Protein acetylation is emerging as a major mechanism by which key proteins are regulated in many physiological processes such as migration, metabolism and aging as well as in pathological circumstances such as cancer and neurodegenerative disorders.

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Figures

Fig. 1
Fig. 1
Physiological and physiopathological roles of acetylation or deacetylation of non-nuclear substrates. Deacetylases (sirtuins and HDAC6, in black) and the acetylase ELP3 (in red) are represented with their respective substrates. The biological significance of acetylation or deacetylation of these substrates is indicated. Updated from [102]
Fig. 2
Fig. 2
Pathways regulated by some sirtuins and HDAC6 in the mitochondria and in the cytoplasm. Substrates of SIRT1, 2, 3 and 5 as well of HDAC6 are illustrated. These pathways regulate the actin cytoskeleton, microtubule (de)acetylations, TCA and urea cycles as well as levels of fatty acids (see text for details)
See this image and copyright information in PMC

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