The human protein PRR14 tethers heterochromatin to the nuclear lamina during interphase and mitotic exit.

The human protein PRR14 tethers heterochromatin to the nuclear lamina during interphase and mitotic exit.
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DOI:
10.1016/j.celrep.2013.09.024
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发表时间:
2013-10-31
期刊:
影响因子:
8.8
通讯作者:
Katz RA
Katz RA
中科院分区:
生物学1区
文献类型:
--
作者:
Poleshko A;Mansfield KM;Burlingame CC;Andrake MD;Shah NR;Katz RA

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核膜是位于后生动物细胞内核膜下的蛋白质网。核层的一个功能是在核内边缘组织异染色质。然而,对于异染色质如何附着在核层上以及这种附着如何在有丝分裂结束时恢复,人们知之甚少。在这里,我们发现了一种以前未被研究过的人类蛋白PRR14,通过与异染色质蛋白1 (HP1)和核层的关联,在间期将异染色质连接到核外周。在有丝分裂早期,PRR14从核层和染色质中释放出来,并保持可溶性。引人注目的是,在后期开始时,PRR14通过HP1结合迅速结合到染色质中。最后,在末期,PRR14重新定位到重组核层。PRR14的这种分步重组表明,当细胞有丝分裂结束时,选择与hp1结合的异染色质重新附着在核层上具有一种新的功能。
The nuclear lamina is a protein meshwork that lies under the inner nuclear membrane of metazoan cells. One function of the nuclear lamina is to organize heterochromatin at the inner nuclear periphery. However, very little is known about how heterochromatin attaches to the nuclear lamina and how such attachments are restored at mitotic exit. Here we show that a previously unstudied human protein, PRR14, functions to tether heterochromatin to the nuclear periphery during interphase, through associations with heterochromatin protein 1 (HP1) and the nuclear lamina. During early mitosis, PRR14 is released from the nuclear lamina and chromatin, and remains soluble. Strikingly, at the onset of anaphase, PRR14 is incorporated rapidly into chromatin through HP1 binding. Finally, in telophase, PRR14 relocalizes to the reforming nuclear lamina. This stepwise reassembly of PRR14 suggests a novel function in the selection of HP1–bound heterochromatin for reattachment to the nuclear lamina as cells exit mitosis.
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