title: 4D-networking by mitotic phosphatases.
abstract: Faithful progression through mitosis is critically dependent on the timely phosphorylation and dephosphorylation of a host of proteins. The involved protein kinases and phosphatases are embedded in interconnected feedback and feedforward circuits that ensure swift and robust phase transitions. Here we review recent evidence showing that protein phosphatases are modulators of the mitotic entry but also organize the mitotic exit through an orderly dephosphorylation of their substrates. In addition, phosphatases spatiotemporally restrict the phosphorylation of key regulatory proteins and oppose kinases to control highly dynamic mitotic processes, including chromosome congression and checkpoint signaling. In accordance with their important role as nodes in phosphorylation networks, mitotic protein phosphatases are tightly regulated in four dimensions.
authors.affiliation: Laboratory of Biosignaling & Therapeutics, Department of Cellular and Molecular Medicine, University of Leuven, B-3000 Leuven, Belgium.
authors.forename: Junbin
authors.initials: J
authors.lastname: Qian
authors.forename: Claudia
authors.initials: C
authors.lastname: Winkler
authors.forename: Mathieu
authors.initials: M
authors.lastname: Bollen
mesh_terms: D000818:Animals; D006801:Humans; D053858:Metabolic Networks and Pathways; D008938:Mitosis; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism
chemical_list: D011494:Protein Kinases; D010749:Phosphoprotein Phosphatases