Closing a gap in the nuclear envelope

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• 作者：Marina Vietri¹ ; ² ; Harald Stenmark¹ ; ² ; ³ ; ^{stenmark@ulrik.uio.no" class="auth_mail" title="E-mail the corresponding author} ; Coen Campsteijn¹ ; ² ; ^{coen.campsteijn@rr-research.no" class="auth_mail" title="E-mail the corresponding author}
• 刊名：Current Opinion in Cell Biology
• 出版年：2016
• 出版时间：June 2016
• 年：2016
• 卷：40
• 期：Complete
• 页码：90-97
• 全文大小：873 K

文摘

The nuclear envelope (NE) ensures nucleo-cytoplasmic compartmentalization, with trafficking of macromolecules across this double membrane controlled by embedded nuclear pore complexes (NPCs). The NE and associated proteins are dismantled during open mitosis and reestablishment of this barrier during mitotic exit requires dynamic remodeling of endoplasmic reticulum (ER) membranes and coordination with NPC reformation, with NPC deposition continuing during subsequent interphase. In this review, we discuss recent progress in our understanding of NE reformation and nuclear pore complex generation, with special focus on work implicating the endosomal sorting complex required for transport (ESCRT) membrane remodeling machinery in these events.