Cargando…
Stepwise reassembly of the nuclear envelope at the end of mitosis
The nuclear envelope consists of three distinct membrane domains: the outer membrane with the bound ribosomes, the inner membrane with the bound lamina, and the pore membrane with the bound pore complexes. Using biochemical and morphological methods, we observed that the nuclear membranes of HeLa ce...
Formato: | Texto |
---|---|
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1993
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2119651/ https://www.ncbi.nlm.nih.gov/pubmed/8391536 |
_version_ | 1782141310463901696 |
---|---|
collection | PubMed |
description | The nuclear envelope consists of three distinct membrane domains: the outer membrane with the bound ribosomes, the inner membrane with the bound lamina, and the pore membrane with the bound pore complexes. Using biochemical and morphological methods, we observed that the nuclear membranes of HeLa cells undergoing mitosis are disassembled in a domain-specific manner, i.e., integral membrane proteins representing the inner nuclear membrane (the lamin B receptor) and the nuclear pore membrane (gp210) are segregated into different populations of mitotic vesicles. At the completion of mitosis, the inner nuclear membrane- derived vesicles associate with chromatin first, beginning in anaphase, whereas the pore membranes and the lamina assemble later, during telophase and cytokinesis. Our data suggest that the ordered reassembly of the nuclear envelope is triggered by the early attachment of inner nuclear membrane-derived vesicles to the chromatin. |
format | Text |
id | pubmed-2119651 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1993 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21196512008-05-01 Stepwise reassembly of the nuclear envelope at the end of mitosis J Cell Biol Articles The nuclear envelope consists of three distinct membrane domains: the outer membrane with the bound ribosomes, the inner membrane with the bound lamina, and the pore membrane with the bound pore complexes. Using biochemical and morphological methods, we observed that the nuclear membranes of HeLa cells undergoing mitosis are disassembled in a domain-specific manner, i.e., integral membrane proteins representing the inner nuclear membrane (the lamin B receptor) and the nuclear pore membrane (gp210) are segregated into different populations of mitotic vesicles. At the completion of mitosis, the inner nuclear membrane- derived vesicles associate with chromatin first, beginning in anaphase, whereas the pore membranes and the lamina assemble later, during telophase and cytokinesis. Our data suggest that the ordered reassembly of the nuclear envelope is triggered by the early attachment of inner nuclear membrane-derived vesicles to the chromatin. The Rockefeller University Press 1993-07-02 /pmc/articles/PMC2119651/ /pubmed/8391536 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles Stepwise reassembly of the nuclear envelope at the end of mitosis |
title | Stepwise reassembly of the nuclear envelope at the end of mitosis |
title_full | Stepwise reassembly of the nuclear envelope at the end of mitosis |
title_fullStr | Stepwise reassembly of the nuclear envelope at the end of mitosis |
title_full_unstemmed | Stepwise reassembly of the nuclear envelope at the end of mitosis |
title_short | Stepwise reassembly of the nuclear envelope at the end of mitosis |
title_sort | stepwise reassembly of the nuclear envelope at the end of mitosis |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2119651/ https://www.ncbi.nlm.nih.gov/pubmed/8391536 |