Shou W, Seol J H, Shevchenko A, Baskerville C, Moazed D, Chen Z W, Jang J, Shevchenko A, Charbonneau H, Deshaies R J
Division of Biology, California Institute of Technology, Pasadena, California 91125, USA.
Cell. 1999 Apr 16;97(2):233-44. doi: 10.1016/s0092-8674(00)80733-3.
Exit from mitosis in budding yeast requires a group of essential proteins--including the GTPase Tem1 and the protein phosphatase Cdc14--that downregulate cyclin-dependent kinase activity. We identified a mutation, net1-1, that bypasses the lethality of tem1 delta. NET1 encodes a novel protein, and mass spectrometric analysis reveals that it is a key component of a multifunctional complex, denoted RENT (for regulator of nucleolar silencing and telophase), that also contains Cdc14 and the silencing regulator Sir2. From G1 through anaphase, RENT localizes to the nucleolus, and Cdc14 activity is inhibited by Net1. In late anaphase, Cdc14 dissociates from RENT, disperses throughout the cell in a Tem1-dependent manner, and ultimately triggers mitotic exit. Nucleolar sequestration may be a general mechanism for the regulation of diverse biological processes.
芽殖酵母从有丝分裂中退出需要一组必需蛋白质——包括GTP酶Tem1和蛋白磷酸酶Cdc14——这些蛋白质会下调细胞周期蛋白依赖性激酶的活性。我们鉴定出一个突变体net1-1，它能绕过tem1δ的致死性。NET1编码一种新型蛋白质，质谱分析表明它是一个多功能复合物的关键组分，该复合物称为RENT（核仁沉默与末期调节因子），它还包含Cdc14和沉默调节因子Sir2。从G1期到后期，RENT定位于核仁，Net1会抑制Cdc14的活性。在后期末，Cdc14从RENT上解离，以Tem1依赖的方式分散到整个细胞中，并最终触发有丝分裂退出。核仁隔离可能是调节多种生物学过程的一种普遍机制。
