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Lookup NU author(s): Emeritus Professor Nick Europe-Finner,
Professor Michael Taggart,
Dr Magdalena Karolczak-Bayatti
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
Post-translational modifications (PTMs) of proteins by phosphorylation are a well-established mechanism by which their activities can be regulated to affect cellular physiology. However, it is becoming increasingly evident that PTMs of proteins by acetylation of lysine residues is also a key effecter in regulating their functional abilities. The best characterized case of this is the epigenetic effects of histone acetyltransferases and deacetylases on gene expression via modulation of nuclear histone acetylation and chro- matin remodeling. However, recent published evidence now strongly implicates an important role for nonhistone acetylation in regulating cellular function. In this review, we have considered the potential for regulating myometrial activity not only by epige- netic mechanisms but also by nonepigenetic protein acetylation processes that could directly affect the contractile machinery within these smooth muscle cells.
Author(s): Europe-Finner GN, Taggart MJ, Karolczak-Bayatti M
Publication type: Article
Publication status: Published
Journal: Reproductive Sciences
Print publication date: 12/03/2012
ISSN (print): 1933-7191
ISSN (electronic): 1933-7205
Publisher: Sage Publications, Inc.
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