Review

Nature Reviews Molecular Cell Biology 8, 234-244 (March 2007) | doi:10.1038/nrm2126

Emerging roles of nuclear protein phosphatases

Greg B. G. Moorhead1, Laura Trinkle-Mulcahy2 & Annegret Ulke-Lemée1  About the authors

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The phosphorylation state of any protein represents a balance of the actions of specific protein kinases and protein phosphatases. Many protein phosphatases are highly enriched in, or exclusive to, the nuclear compartment, where they dephosphorylate key substrates to regulate various nuclear processes. In this review we will discuss recent findings that define the role of nuclear protein phosphatases in controlling transforming growth factor-beta (TGFbeta) and bone-morphogenetic protein (BMP) signalling, the DNA-damage response, RNA processing, cell-cycle progression and gene transcription.

Author affiliations

  1. Department of Biological Sciences, University of Calgary, 2500 University Drive NW, Calgary Alberta, Canada T2N 1N4.
  2. MSI/WTB Complex, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland.

Correspondence to: Greg B. G. Moorhead1 Email: moorhead@ucalgary.ca

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