title: Wip1-dependent signaling pathways in health and diseases.
abstract: Spatial and temporal regulation of protein phosphorylation is key to the control of different molecular networks. This regulation is achieved in part through dephosphorylation of numerous signaling molecules, and emerging evidence highlights the importance of a new member of the PP2C family of phosphatase, Wild-type p53 induced phosphatase 1 (Wip1), in regulating stress-induced and DNA damage-induced networks. In recent years, analysis of Wip1 has focused primarily on its role in tumorigenesis because of its overexpression in human tumors and a profound tumor-resistant phenotype of Wip1-deficient mice. Recently, Wip1 has also been shown to play an important role in several physiological processes including adult neurogenesis and organismal aging. This review addresses how Wip1 phosphatase regulates different signaling networks in a spatial and temporal manner and how these differences contribute to various biological outcomes in the context of physiological and pathological conditions.
authors.affiliation: Cell Cycle Control and Tumorigenesis Group, Institute of Molecular and Cell Biology, Proteos, Singapore.
authors.forename: Yun-Hua
authors.initials: YH
authors.lastname: Zhu
authors.forename: Dmitry V
authors.initials: DV
authors.lastname: Bulavin
mesh_terms: D000375:Aging / Q000502:physiology*; D000818:Animals; D064007:Ataxia Telangiectasia Mutated Proteins; D002453:Cell Cycle / Q000502:physiology; D018797:Cell Cycle Proteins / Q000502:physiology; D002471:Cell Transformation, Neoplastic; D004268:DNA-Binding Proteins / Q000502:physiology; D004789:Enzyme Activation; D006801:Humans; D008297:Male; D051379:Mice; D016328:NF-kappa B / Q000502:physiology; D009363:Neoplasm Proteins / Q000502:physiology; D009369:Neoplasms / Q000201:enzymology / Q000209:etiology / Q000517:prevention & control; D009419:Nerve Tissue Proteins / Q000502:physiology; D055495:Neurogenesis / Q000502:physiology*; D010749:Phosphoprotein Phosphatases / Q000172:deficiency / Q000235:genetics / Q000502:physiology*; D010750:Phosphoproteins / Q000378:metabolism; D010766:Phosphorylation; D000071636:Protein Phosphatase 2C; D011499:Protein Processing, Post-Translational; D017346:Protein Serine-Threonine Kinases / Q000502:physiology; D015398:Signal Transduction / Q000502:physiology*; D013234:Stem Cells / Q000166:cytology / Q000201:enzymology; D016159:Tumor Suppressor Protein p53 / Q000502:physiology; D025521:Tumor Suppressor Proteins / Q000502:physiology; D048051:p38 Mitogen-Activated Protein Kinases / Q000502:physiology
chemical_list: D018797:Cell Cycle Proteins; D004268:DNA-Binding Proteins; D016328:NF-kappa B; D009363:Neoplasm Proteins; D009419:Nerve Tissue Proteins; D010750:Phosphoproteins; D016159:Tumor Suppressor Protein p53; D025521:Tumor Suppressor Proteins; C576324:ATM protein, human; D064007:Ataxia Telangiectasia Mutated Proteins; C576325:Atm protein, mouse; D017346:Protein Serine-Threonine Kinases; D048051:p38 Mitogen-Activated Protein Kinases; C000607458:PPM1D protein, human; D010749:Phosphoprotein Phosphatases; C000607468:Ppm1d protein, mouse; D000071636:Protein Phosphatase 2C