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A role for cytoskeletal protein acetylation in modulating myometrial activity

Lookup NU author(s): Emeritus Professor Nick Europe-Finner, Professor Michael TaggartORCiD, Dr Magdalena Karolczak-Bayatti


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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.

Publication metadata

Author(s): Europe-Finner GN, Taggart MJ, Karolczak-Bayatti M

Publication type: Article

Publication status: Published

Journal: Reproductive Sciences

Year: 2013

Volume: 20

Issue: 2

Pages: 175-181

Print publication date: 12/03/2012

ISSN (print): 1933-7191

ISSN (electronic): 1933-7205

Publisher: Sage Publications, Inc.


DOI: 10.1177/1933719111432876


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Funder referenceFunder name
G0800202Medical Research Council (UK)
G0900525Medical Research Council (UK)
PG/09/075British Heart Foundation