Meiosis‐specific cohesin component, Rec8, promotes the localization of Mps3 SUN domain protein on the nuclear envelope

Meiosis‐specific cohesin component, Rec8, promotes the localization of Mps3 SUN domain protein on the nuclear envelope
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减数分裂特异性粘连蛋白成分 Rec8 促进 Mps3 SUN 结构域蛋白在核膜上的定位

DOI:
10.1111/gtc.12653
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发表时间:
2018
期刊:
影响因子:
2.1
通讯作者:
Shinohara Akira
Shinohara Akira
中科院分区:
生物学4区
文献类型:
--
作者:
Bommi Jagadeeswara Rao;Rao Hanumanthu Bala Durga Prasada;Challa Kiran;Higashide Mika;Shinmyozu Kaori;Nakayama Jun‐ichi;Shinohara Miki;Shinohara Akira

文献摘要

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核膜中的蛋白质在有丝分裂和减数分裂过程中对细胞核和染色体的动态和功能起着重要作用。Mps3是一种酵母NE蛋白,具有保守的SUN结构域,主要定位于有丝分裂细胞中与酵母中心体相当的纺锤体极体(SPB)上。在减数分裂过程中,Mps3与Spb一起在NE上形成了一个明显的多重系综。Mps3的减数分裂特异性去甲肾上腺素(NE)定位是如何调控的,目前仍不清楚。在这项研究中,我们发现在减数分裂过程中,姐妹染色单体凝聚所必需的蛋白质复合体的减数分裂特异成分Rec8与Mps3结合,并控制Mps3在NE上的定位和适当的动力学。REC8在有丝分裂酵母细胞中的异位表达诱导NE上形成Mps3斑块/焦点。这需要粘附素调节因子,WAPL同源基因,Rad61/Wpl1,这表明减数分裂特异的粘附素复合体与Rec8控制Mps3的NE定位。我们还观察到Mps3核质区的两个区域对于Mps3在有丝分裂和减数分裂细胞中的去甲肾上腺素定位是必不可少的。我们推测,Mps3与核质中减数分裂特异的粘附素的相互作用是Mps3去甲肾上腺素定位/功能的关键决定因素。
Proteins in the nuclear envelope (NE) play a role in the dynamics and functions of the nucleus and of chromosomes during mitosis and meiosis. Mps3, a yeast NE protein with a conserved SUN domain, predominantly localizes on a yeast centrosome equivalent, spindle pole body (SPB), in mitotic cells. During meiosis, Mps3, together with SPB, forms a distinct multiple ensemble on NE. How meiosis‐specific NE localization of Mps3 is regulated remains largely unknown. In this study, we found that a meiosis‐specific component of the protein complex essential for sister chromatid cohesion, Rec8, binds to Mps3 during meiosis and controls Mps3 localization and proper dynamics on NE. Ectopic expression of Rec8 in mitotic yeast cells induced the formation of Mps3 patches/foci on NE. This required the cohesin regulator, WAPL ortholog, Rad61/Wpl1, suggesting that a meiosis‐specific cohesin complex with Rec8 controls NE localization of Mps3. We also observed that two domains of the nucleoplasmic region of Mps3 are essential for NE localization of Mps3 in mitotic as well as meiotic cells. We speculate that the interaction of Mps3 with the meiosis‐specific cohesin in the nucleoplasm is a key determinant for NE localization/function of Mps3.