Cargando…
The intriguing plant nuclear lamina
The nuclear lamina is a complex protein mesh attached to the inner nuclear membrane (INM), which is also associated with nuclear pore complexes. It provides mechanical support to the nucleus and nuclear envelope, and as well as facilitating the connection of the nucleoskeleton to the cytoskeleton, i...
Autores principales: | , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4010787/ https://www.ncbi.nlm.nih.gov/pubmed/24808902 http://dx.doi.org/10.3389/fpls.2014.00166 |
_version_ | 1782479907603873792 |
---|---|
author | Ciska, Malgorzata Moreno Díaz de la Espina, Susana |
author_facet | Ciska, Malgorzata Moreno Díaz de la Espina, Susana |
author_sort | Ciska, Malgorzata |
collection | PubMed |
description | The nuclear lamina is a complex protein mesh attached to the inner nuclear membrane (INM), which is also associated with nuclear pore complexes. It provides mechanical support to the nucleus and nuclear envelope, and as well as facilitating the connection of the nucleoskeleton to the cytoskeleton, it is also involved in chromatin organization, gene regulation, and signaling. In metazoans, the nuclear lamina consists of a polymeric layer of lamins and other interacting proteins responsible for its association with the INM and chromatin. In plants, field emission scanning electron microscopy of nuclei, and thin section transmission electron microscopy of isolated nucleoskeletons, reveals the lamina to have a similar structure to that of metazoans. Moreover, although plants lack lamin genes and the genes encoding most lamin-binding proteins, the main functions of the lamina are fulfilled in plants. Hence, it would appear that the plant lamina is not based on lamins and that other proteins substitute for lamins in plant cells. The nuclear matrix constituent proteins are the best characterized structural proteins in the plant lamina. Although these proteins do not display strong sequence similarity to lamins, their predicted secondary structure and sub-nuclear distribution, as well as their influence on nuclear size and shape, and on heterochromatin organization, suggest they could be functional lamin analogs. In this review we shall summarize what is currently known about the organization and composition of the plant nuclear lamina and its interacting complexes, and we will discuss the activity of this structure in the plant cell and its nucleus. |
format | Online Article Text |
id | pubmed-4010787 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-40107872014-05-07 The intriguing plant nuclear lamina Ciska, Malgorzata Moreno Díaz de la Espina, Susana Front Plant Sci Plant Science The nuclear lamina is a complex protein mesh attached to the inner nuclear membrane (INM), which is also associated with nuclear pore complexes. It provides mechanical support to the nucleus and nuclear envelope, and as well as facilitating the connection of the nucleoskeleton to the cytoskeleton, it is also involved in chromatin organization, gene regulation, and signaling. In metazoans, the nuclear lamina consists of a polymeric layer of lamins and other interacting proteins responsible for its association with the INM and chromatin. In plants, field emission scanning electron microscopy of nuclei, and thin section transmission electron microscopy of isolated nucleoskeletons, reveals the lamina to have a similar structure to that of metazoans. Moreover, although plants lack lamin genes and the genes encoding most lamin-binding proteins, the main functions of the lamina are fulfilled in plants. Hence, it would appear that the plant lamina is not based on lamins and that other proteins substitute for lamins in plant cells. The nuclear matrix constituent proteins are the best characterized structural proteins in the plant lamina. Although these proteins do not display strong sequence similarity to lamins, their predicted secondary structure and sub-nuclear distribution, as well as their influence on nuclear size and shape, and on heterochromatin organization, suggest they could be functional lamin analogs. In this review we shall summarize what is currently known about the organization and composition of the plant nuclear lamina and its interacting complexes, and we will discuss the activity of this structure in the plant cell and its nucleus. Frontiers Media S.A. 2014-04-29 /pmc/articles/PMC4010787/ /pubmed/24808902 http://dx.doi.org/10.3389/fpls.2014.00166 Text en Copyright © 2014 Ciska and Moreno Díaz de la Espina. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Plant Science Ciska, Malgorzata Moreno Díaz de la Espina, Susana The intriguing plant nuclear lamina |
title | The intriguing plant nuclear lamina |
title_full | The intriguing plant nuclear lamina |
title_fullStr | The intriguing plant nuclear lamina |
title_full_unstemmed | The intriguing plant nuclear lamina |
title_short | The intriguing plant nuclear lamina |
title_sort | intriguing plant nuclear lamina |
topic | Plant Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4010787/ https://www.ncbi.nlm.nih.gov/pubmed/24808902 http://dx.doi.org/10.3389/fpls.2014.00166 |
work_keys_str_mv | AT ciskamalgorzata theintriguingplantnuclearlamina AT morenodiazdelaespinasusana theintriguingplantnuclearlamina AT ciskamalgorzata intriguingplantnuclearlamina AT morenodiazdelaespinasusana intriguingplantnuclearlamina |