Degradation of the kinesin Kip1p at anaphase onset is mediated by the anaphase-promoting complex and Cdc20p
Degradation of the kinesin Kip1p at anaphase onset is mediated by the anaphase-promoting complex and Cdc20p
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DOI：
10.1073/pnas.231212498
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发表时间：
2001-10-23
影响因子：
11.1
通讯作者：
Roof, DM
中科院分区：
文献类型：
--
作者：
Gordon, DM;Roof, DM
酿酒酵母的 Kip1p 是保守的 bimC 驱动蛋白亚家族中的双极驱动蛋白，介导有丝分裂纺锤体-极分离。在这里，我们表明 Kip1p 在后期启动后立即通过其快速降解受到调节。降解需要称为后期促进复合物的泛素蛋白连接酶、后期促进复合物激活蛋白 Cdc20 以及 Kip1p 中独特的 43 个氨基酸序列。降解也需要 Kip1p 进入细胞核，但发生与纺锤体关联无关。稳定 Kip1p 的突变损害了后期进展。降解时间表明 Kip1p 主要在纺锤体组装和中期发挥作用，并且随着后期的进展，Kip1p 降解促进有丝分裂纺锤体的结构变化。
Kip1p ofSaccharomyces cerevisiaeis a bipolar kinesin in the conserved bimC kinesin subfamily that mediates mitotic spindle–pole separation. Here, we show that Kip1p is regulated immediately after anaphase initiation by its rapid degradation. Degradation required the ubiquitin protein ligase called the anaphase-promoting complex, the anaphase-promoting complex activating protein Cdc20, and a unique 43-aa sequence in Kip1p. Degradation also required import of Kip1p into the nucleus, but occurred independently of spindle association. A mutation that stabilized Kip1p impaired anaphase progression. The timing of degradation suggests that Kip1p functions primarily during spindle assembly and metaphase, and that Kip1p degradation facilitates structural changes in the mitotic spindle as anaphase progresses.