Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo.
Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo.
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DOI:
10.1083/jcb.200901106
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发表时间:
2009-07-27
期刊:
影响因子:
--
通讯作者:
Hetzer MW
中科院分区:
文献类型:
--
作者:
Anderson DJ;Vargas JD;Hsiao JP;Hetzer MW
Formation of the nuclear envelope (NE) around segregated chromosomes occurs by the reshaping of the endoplasmic reticulum (ER), a reservoir for disassembled nuclear membrane components during mitosis. In this study, we show that inner nuclear membrane proteins such as lamin B receptor (LBR), MAN1, Lap2β, and the trans-membrane nucleoporins Ndc1 and POM121 drive the spreading of ER membranes into the emerging NE via their capacity to bind chromatin in a collaborative manner. Despite their redundant functions, decreasing the levels of any of these trans-membrane proteins by RNAi-mediated knockdown delayed NE formation, whereas increasing the levels of any of them had the opposite effect. Furthermore, acceleration of NE formation interferes with chromosome separation during mitosis, indicating that the time frame over which chromatin becomes membrane enclosed is physiologically relevant and regulated. These data suggest that functionally distinct classes of chromatin-interacting membrane proteins, which are present at nonsaturating levels, collaborate to rapidly reestablish the nuclear compartment at the end of mitosis.
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DOI:
10.1073/pnas.0730821100
发表时间:
2003-04-15
影响因子:
11.1
作者:
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通讯作者:
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影响因子:
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作者:
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DOI:
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发表时间:
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期刊:
The Journal of cell biology
影响因子:
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作者:
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通讯作者:
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影响因子:
16
作者:
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通讯作者:
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影响因子:
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作者:
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通讯作者:
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