A role for cytoskeletal protein acetylation in modulating myometrial activity

  1. Lookup NU author(s)
  2. Professor Nick Europe-Finner
  3. Professor Michael Taggart
  4. Dr Magdalena Karolczak-Bayatti
Author(s)Europe-Finner GN, Taggart MJ, Karolczak-Bayatti M
Publication type Article
JournalReproductive Sciences
ISSN (print)1933-7191
ISSN (electronic)1933-7205
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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.
PublisherSage Publications, Inc.
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