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Regulation and coordination of nuclear envelope and nuclear pore complex assembly

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...

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Autores principales: Clever, Michaela, Mimura, Yasuhiro, Funakoshi, Tomoko, Imamoto, Naoko
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Landes Bioscience 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3621742/
https://www.ncbi.nlm.nih.gov/pubmed/23412657
http://dx.doi.org/10.4161/nucl.23796
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author Clever, Michaela
Mimura, Yasuhiro
Funakoshi, Tomoko
Imamoto, Naoko
author_facet Clever, Michaela
Mimura, Yasuhiro
Funakoshi, Tomoko
Imamoto, Naoko
author_sort Clever, Michaela
collection PubMed
description 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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spelling pubmed-36217422013-04-22 Regulation and coordination of nuclear envelope and nuclear pore complex assembly Clever, Michaela Mimura, Yasuhiro Funakoshi, Tomoko Imamoto, Naoko Nucleus Review 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. Landes Bioscience 2013-03-01 /pmc/articles/PMC3621742/ /pubmed/23412657 http://dx.doi.org/10.4161/nucl.23796 Text en Copyright © Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
spellingShingle Review
Clever, Michaela
Mimura, Yasuhiro
Funakoshi, Tomoko
Imamoto, Naoko
Regulation and coordination of nuclear envelope and nuclear pore complex assembly
title Regulation and coordination of nuclear envelope and nuclear pore complex assembly
title_full Regulation and coordination of nuclear envelope and nuclear pore complex assembly
title_fullStr Regulation and coordination of nuclear envelope and nuclear pore complex assembly
title_full_unstemmed Regulation and coordination of nuclear envelope and nuclear pore complex assembly
title_short Regulation and coordination of nuclear envelope and nuclear pore complex assembly
title_sort regulation and coordination of nuclear envelope and nuclear pore complex assembly
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3621742/
https://www.ncbi.nlm.nih.gov/pubmed/23412657
http://dx.doi.org/10.4161/nucl.23796
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