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Updated: May 14, 2026

Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner
Published on: December 10, 2015
Regulation and coordination of nuclear envelope and nuclear pore complex assembly
Michaela Clever1, Yasuhiro Mimura, Tomoko Funakoshi
1Cellular Dynamics Laboratory, RIKEN Advanced Science Institute 2-1 Hirosawa, Wako, Japan.
Abstract:
In metazoans with "open" mitosis, cells undergo structural changes involving the complete disassembly of the nuclear envelope (NE). In post-mitosis, the dividing cell faces the difficulty to reassemble NE structures in a highly regulated fashion around separated chromosomes. The de novo formation of nuclear pore complexes (NPCs), which are gateways between the cytoplasm and nucleoplasm across the nuclear membrane, is an archetype of macromolecular assembly and is therefore of special interest. The reformation of a functional NE further involves the reassembly and organization of other NE components, the nuclear membrane and NE proteins, around chromosomes in late mitosis. Here, we discuss the function of NE components, such as lamins and INM proteins, in NE reformation and highlight recent results on coordination of NPC and NE assembly.
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