Csi1p recruits alp7p/TACC to the spindle pole bodies for bipolar spindle formation.
Csi1p recruits alp7p/TACC to the spindle pole bodies for bipolar spindle formation.
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Csi1p 将 alp7p/TACC 募集至纺锤体极体，形成双极纺锤体。
DOI：
10.1091/mbc.e14-03-0786
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发表时间：
2014-09-15
影响因子：
3.3
通讯作者：
Fu C
中科院分区：
文献类型：
--
作者：
Zheng F;Li T;Jin DY;Syrovatkina V;Scheffler K;Tran PT;Fu C
裂殖酵母裂殖酵母TACC直向同源物alp 7 p的纺锤体极体（SPB）定位依赖于SPB蛋白csi 1 p。csi 1 p和alp 7 p之间相互作用的减弱延迟了双极纺锤体的形成并导致染色体异常分离。准确的染色体分离需要在有丝分裂过程中及时形成双极纺锤体。转化酸性卷曲螺旋（TACC）家族蛋白和ch-TOG家族蛋白是双极纺锤体形成的关键参与者。它们形成复合物以稳定纺锤体微管，主要依赖于它们在中心体（酵母中的纺锤体极体[SPB]）的定位。TACC-ch-TOG复合物靶向中心体的分子机制尚不清楚。在这里，我们表明，裂变酵母裂殖酵母粟酒裂殖酵母TACC直向同源alp 7 p招募的SPB的csi 1 p。csi 1 p相互作用区域位于alp 7 p的保守TACC结构域内，csi 1 p的羧基末端结构域负责与alp 7 p相互作用。csi 1 p和alp 7 p之间的相互作用受损的有丝分裂过程中的SP B的alp 7 p的本地化，从而延迟双极纺锤体的形成，并导致后期B落后的染色体。因此，我们的研究表明，csi 1 p作为一个连接分子拴纺锤体稳定因子的SPB促进双极纺锤体组装。
The spindle pole body (SPB) localization of the fission yeast Schizosaccharomyces pombe TACC orthologue alp7p depends on the SPB protein csi1p. Compromised interaction between csi1p and alp7p delays bipolar spindle formation and leads to abnormal chromosome segregation. Accurate chromosome segregation requires timely bipolar spindle formation during mitosis. The transforming acidic coiled-coil (TACC) family proteins and the ch-TOG family proteins are key players in bipolar spindle formation. They form a complex to stabilize spindle microtubules, mainly dependent on their localization to the centrosome (the spindle pole body [SPB] in yeast). The molecular mechanism underlying the targeting of the TACC–ch-TOG complex to the centrosome remains unclear. Here we show that the fission yeast Schizosaccharomyces pombe TACC orthologue alp7p is recruited to the SPB by csi1p. The csi1p-interacting region lies within the conserved TACC domain of alp7p, and the carboxyl-terminal domain of csi1p is responsible for interacting with alp7p. Compromised interaction between csi1p and alp7p impairs the localization of alp7p to the SPB during mitosis, thus delaying bipolar spindle formation and leading to anaphase B lagging chromosomes. Hence our study establishes that csi1p serves as a linking molecule tethering spindle-stabilizing factors to the SPB for promoting bipolar spindle assembly.