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Displacement affinity chromatography of protein phosphatase one (PP1) complexes |
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| Authors: | Greg BG Moorhead Laura Trinkle-Mulcahy Mhairi Nimick Veerle De Wever David G Campbell Robert Gourlay Yun Wah Lam Angus I Lamond |
| Institution: | (1) Department of Biological Sciences, University of Calgary, 2500 University Dr. N.W, Calgary, AB, T2N 1N4, Canada;(2) Wellcome Trust Biocentre, MSI/WTB Complex, University of Dundee, Dundee, DD1 5EH, UK;(3) MRC Protein Phosphorylation Unit, School of Life Sciences, University of Dundee, Dundee, Scotland, DD1 5EH, UK |
| Abstract: | BackgroundProtein phosphatase one (PP1) is a ubiquitously expressed, highly conserved protein phosphatase that dephosphorylates target protein serine and threonine residues. PP1 is localized to its site of action by interacting with targeting or regulatory proteins, a majority of which contains a primary docking site referred to as the RVXF/W motif. |
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