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Tem1 定位于纺锤体极体对于有丝分裂退出是必不可少的，并损害了纺锤体检验点功能。

Tem1 localization to the spindle pole bodies is essential for mitotic exit and impairs spindle checkpoint function.

机构信息

Centro Andaluz de Biología Molecular y Medicina Regenerativa (CABIMER), Universidad de Sevilla, Sevilla, Spain.

出版信息

J Cell Biol. 2011 Feb 21;192(4):599-614. doi: 10.1083/jcb.201007044. Epub 2011 Feb 14.

DOI:10.1083/jcb.201007044
PMID:21321099
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3044116/
Abstract

The mitotic exit network (MEN) is a signaling cascade that triggers inactivation of the mitotic cyclin-dependent kinases and exit from mitosis. The GTPase Tem1 localizes on the spindle pole bodies (SPBs) and initiates MEN signaling. Tem1 activity is inhibited until anaphase by Bfa1-Bub2. These proteins are also part of the spindle position checkpoint (SPOC), a surveillance mechanism that restrains mitotic exit until the spindle is correctly positioned. Here, we show that regulation of Tem1 localization is essential for the proper function of the MEN and the SPOC. We demonstrate that the dynamics of Tem1 loading onto SPBs determine the recruitment of other MEN components to this structure, and reevaluate the interdependence in the localization of Tem1, Bfa1, and Bub2. We also find that removal of Tem1 from the SPBs is critical for the SPOC to impede cell cycle progression. Finally, we demonstrate for the first time that localization of Tem1 to the SPBs is a requirement for mitotic exit.

摘要

有丝分裂退出网络（MEN）是一个信号级联反应，它触发有丝分裂周期蛋白依赖性激酶的失活并退出有丝分裂。GTP 酶 Tem1 定位于纺锤体极体（SPB）上，并启动 MEN 信号。Tem1 的活性被 Bfa1-Bub2 抑制，直到后期。这些蛋白质也是纺锤体位置检查点（SPOC）的一部分，SPOC 是一种监控机制，它抑制有丝分裂退出，直到纺锤体正确定位。在这里，我们表明 Tem1 定位的调节对于 MEN 和 SPOC 的正常功能是必不可少的。我们证明 Tem1 加载到 SPB 上的动力学决定了其他 MEN 成分向该结构的招募，并重新评估 Tem1、Bfa1 和 Bub2 定位的相互依赖性。我们还发现，从 SPB 上除去 Tem1 对于 SPOC 阻止细胞周期进程至关重要。最后，我们首次证明 Tem1 定位于 SPB 是有丝分裂退出的一个要求。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/13f3/3044116/86ca00da99e0/JCB_201007044_RGB_Fig7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/13f3/3044116/8b31092bd9ae/JCB_201007044_RGB_Fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/13f3/3044116/3a5db39e6d9c/JCB_201007044_RGB_Fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/13f3/3044116/b6fcfd71ab09/JCB_201007044_RGB_Fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/13f3/3044116/7f0ca45d1d59/JCB_201007044_RGB_Fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/13f3/3044116/03779f503da8/JCB_201007044_GS_Fig5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/13f3/3044116/93b39077fbf4/JCB_201007044_RGB_Fig6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/13f3/3044116/86ca00da99e0/JCB_201007044_RGB_Fig7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/13f3/3044116/8b31092bd9ae/JCB_201007044_RGB_Fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/13f3/3044116/3a5db39e6d9c/JCB_201007044_RGB_Fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/13f3/3044116/b6fcfd71ab09/JCB_201007044_RGB_Fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/13f3/3044116/7f0ca45d1d59/JCB_201007044_RGB_Fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/13f3/3044116/03779f503da8/JCB_201007044_GS_Fig5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/13f3/3044116/93b39077fbf4/JCB_201007044_RGB_Fig6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/13f3/3044116/86ca00da99e0/JCB_201007044_RGB_Fig7.jpg

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