Functional diversity of protein phosphatase-1, a cellular economizer and reset button.

By Hugo Ceulemans, M. Bollen. Physiological Reviews, 2004

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From promiscuity to precision: protein phosphatases get a makeover. (2009, background): “The reader is referred to a number of excellent reviews for additional information (Ceulemans and Bollen, 2004; Cohen, 2009; Eichhorn et al., 2008; Janssens et al., 2008; Perrotti and Neviani, 2008).”
Serine/threonine phosphatases: mechanism through structure. (2009, background): “PP1 figures prominently in a wide range of cellular processes, including meiosis and cell division, apoptosis, protein synthesis, metabolism, cytoskeletal reorganization, and the regulation of membrane receptors and channels (Ceulemans and Bollen, 2004; Cohen, 2002).”
Post-translational modifications regulate the ticking of the circadian clock (2007, neutral): “As detailed in several recent reviews, phosphatases evolved along different lines than kinase”
The multifunctional nucleolus (2007, background): “An example in humans involves protein phosphatase 1 (PP1), a ubiquitous serine–threonine phosphatase that regulates many cellular processes, including cell divisio”
Glycogen and its metabolism: some new developments and old themes. (2012, background): “Dephosphorylation of glycogen synthase, and other glycogen-metabolizing enzymes, is thought to be mediated by members of a family of glycogen-associated PP1Gs composed of a catalytic subunit (PP1c) bound to a glycogen-targeting subunit [113,114].”