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Poleshko A , Mansfield KM , Burlingame CC , Andrake MD , Shah NR , Katz RA
The human protein PRR14 tethers heterochromatin to the nuclear lamina during interphase and mitotic exit
Cell Rep. 2013 Oct 31;5(2) :292-301
PMID: 24209742    PMCID: PMC3867587   
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Abstract
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 function in the selection of HP1-bound heterochromatin for reattachment to the nuclear lamina as cells exit mitosis.
Notes
Poleshko, Andrey Mansfield, Katelyn M Burlingame, Caroline C Andrake, Mark D Shah, Neil R Katz, Richard A CA006927/CA/NCI NIH HHS/United States CA071515/CA/NCI NIH HHS/United States DK082498/DK/NIDDK NIH HHS/United States R01 CA071515/CA/NCI NIH HHS/United States R01 DK082498/DK/NIDDK NIH HHS/United States Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't United States Cell Rep. 2013 Oct 31;5(2):292-301. doi: 10.1016/j.celrep.2013.09.024.