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Nucleoplasmic Lamin A/C and Polycomb group of proteins: An evolutionarily conserved interplay
Nuclear lamins are the main components of the nuclear lamina at the nuclear periphery, providing mechanical support to the nucleus. However, recent findings suggest that lamins also reside in the nuclear interior, as a distinct and dynamic pool with critical roles in transcriptional regulation. In o...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Taylor & Francis
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4916880/ https://www.ncbi.nlm.nih.gov/pubmed/26930442 http://dx.doi.org/10.1080/19491034.2016.1157675 |
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author | Marullo, F. Cesarini, E. Antonelli, L. Gregoretti, F. Oliva, G. Lanzuolo, C. |
author_facet | Marullo, F. Cesarini, E. Antonelli, L. Gregoretti, F. Oliva, G. Lanzuolo, C. |
author_sort | Marullo, F. |
collection | PubMed |
description | Nuclear lamins are the main components of the nuclear lamina at the nuclear periphery, providing mechanical support to the nucleus. However, recent findings suggest that lamins also reside in the nuclear interior, as a distinct and dynamic pool with critical roles in transcriptional regulation. In our work we found a functional and evolutionary conserved crosstalk between Lamin A/C and the Polycomb group (PcG) of proteins, this being required for the maintenance of the PcG repressive functions. Indeed, Lamin A/C knock-down causes PcG foci dispersion and defects in PcG-mediated higher order structures, thereby leading to impaired PcG mediated transcriptional repression. By using ad-hoc algorithms for image analysis and PLA approaches we hereby show that PcG proteins are preferentially located in the nuclear interior where they interact with nucleoplasmic Lamin A/C. Taken together, our findings suggest that nuclear components, such as Lamin A/C, functionally interact with epigenetic factors to ensure the correct transcriptional program maintenance. |
format | Online Article Text |
id | pubmed-4916880 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Taylor & Francis |
record_format | MEDLINE/PubMed |
spelling | pubmed-49168802016-07-06 Nucleoplasmic Lamin A/C and Polycomb group of proteins: An evolutionarily conserved interplay Marullo, F. Cesarini, E. Antonelli, L. Gregoretti, F. Oliva, G. Lanzuolo, C. Nucleus Extra Views Nuclear lamins are the main components of the nuclear lamina at the nuclear periphery, providing mechanical support to the nucleus. However, recent findings suggest that lamins also reside in the nuclear interior, as a distinct and dynamic pool with critical roles in transcriptional regulation. In our work we found a functional and evolutionary conserved crosstalk between Lamin A/C and the Polycomb group (PcG) of proteins, this being required for the maintenance of the PcG repressive functions. Indeed, Lamin A/C knock-down causes PcG foci dispersion and defects in PcG-mediated higher order structures, thereby leading to impaired PcG mediated transcriptional repression. By using ad-hoc algorithms for image analysis and PLA approaches we hereby show that PcG proteins are preferentially located in the nuclear interior where they interact with nucleoplasmic Lamin A/C. Taken together, our findings suggest that nuclear components, such as Lamin A/C, functionally interact with epigenetic factors to ensure the correct transcriptional program maintenance. Taylor & Francis 2016-03-01 /pmc/articles/PMC4916880/ /pubmed/26930442 http://dx.doi.org/10.1080/19491034.2016.1157675 Text en © 2016 The Author(s). Published with license by Taylor & Francis Group, LLC http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License http://creativecommons.org/licenses/by-nc/3.0/, which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted. |
spellingShingle | Extra Views Marullo, F. Cesarini, E. Antonelli, L. Gregoretti, F. Oliva, G. Lanzuolo, C. Nucleoplasmic Lamin A/C and Polycomb group of proteins: An evolutionarily conserved interplay |
title | Nucleoplasmic Lamin A/C and Polycomb group of proteins: An evolutionarily conserved interplay |
title_full | Nucleoplasmic Lamin A/C and Polycomb group of proteins: An evolutionarily conserved interplay |
title_fullStr | Nucleoplasmic Lamin A/C and Polycomb group of proteins: An evolutionarily conserved interplay |
title_full_unstemmed | Nucleoplasmic Lamin A/C and Polycomb group of proteins: An evolutionarily conserved interplay |
title_short | Nucleoplasmic Lamin A/C and Polycomb group of proteins: An evolutionarily conserved interplay |
title_sort | nucleoplasmic lamin a/c and polycomb group of proteins: an evolutionarily conserved interplay |
topic | Extra Views |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4916880/ https://www.ncbi.nlm.nih.gov/pubmed/26930442 http://dx.doi.org/10.1080/19491034.2016.1157675 |
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