Knippschild Uwe, Gocht Andreas, Wolff Sonja, Huber Nadine, Löhler Jürgen, Stöter Martin
Department of Visceral and Transplantation Surgery, University of Ulm, Steinhövelstr. 9, 89075 Ulm, Germany.
Cell Signal. 2005 Jun;17(6):675-89. doi: 10.1016/j.cellsig.2004.12.011. Epub 2005 Jan 25.
Phosphorylation of serine, threonine and tyrosine residues by cellular protein kinases plays an important role in the regulation of various cellular processes. The serine/threonine specific casein kinase 1 and 2 protein kinase families--(CK1 and CK2)--were among the first protein kinases that had been described. In recent years our knowledge of the regulation and function of mammalian CK1 kinase family members has rapidly increased. Extracellular stimuli, the subcellular localization of CK1 isoforms, their interaction with various cellular structures and proteins, as well as autophosphorylation and proteolytic cleavage of their C-terminal regulatory domains influence CK1 kinase activity. Mammalian CK1 isoforms phosphorylate many different substrates among them key regulatory proteins involved in the control of cell differentiation, proliferation, chromosome segregation and circadian rhythms. Deregulation and/or the incidence of mutations in the coding sequence of CK1 isoforms have been linked to neurodegenerative diseases and cancer. This review will summarize our current knowledge about the function and regulation of mammalian CK1 isoforms.
细胞蛋白激酶对丝氨酸、苏氨酸和酪氨酸残基的磷酸化在各种细胞过程的调控中起着重要作用。丝氨酸/苏氨酸特异性酪蛋白激酶1和2蛋白激酶家族（CK1和CK2）是最早被描述的蛋白激酶之一。近年来，我们对哺乳动物CK1激酶家族成员的调控和功能的了解迅速增加。细胞外刺激、CK1亚型的亚细胞定位、它们与各种细胞结构和蛋白质的相互作用，以及其C末端调节域的自磷酸化和蛋白水解切割都会影响CK1激酶的活性。哺乳动物CK1亚型可磷酸化许多不同的底物，其中包括参与细胞分化、增殖、染色体分离和昼夜节律控制的关键调节蛋白。CK1亚型编码序列的失调和/或突变发生率与神经退行性疾病和癌症有关。本综述将总结我们目前关于哺乳动物CK1亚型的功能和调控的知识。
