Cargando…
A high-content screen reveals new regulators of nuclear membrane stability
Nuclear membrane rupture is a physiological response to multiple in vivo processes, such as cell migration, that can cause extensive genome instability and upregulate invasive and inflammatory pathways. However, the underlying molecular mechanisms of rupture are unclear and few regulators have been...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10312541/ https://www.ncbi.nlm.nih.gov/pubmed/37398267 http://dx.doi.org/10.1101/2023.05.30.542944 |
_version_ | 1785066947104210944 |
---|---|
author | Gunn, Amanda L. Yashchenko, Artem I. Dubrulle, Julien Johnson, Jodiene Hatch, Emily M. |
author_facet | Gunn, Amanda L. Yashchenko, Artem I. Dubrulle, Julien Johnson, Jodiene Hatch, Emily M. |
author_sort | Gunn, Amanda L. |
collection | PubMed |
description | Nuclear membrane rupture is a physiological response to multiple in vivo processes, such as cell migration, that can cause extensive genome instability and upregulate invasive and inflammatory pathways. However, the underlying molecular mechanisms of rupture are unclear and few regulators have been identified. In this study, we developed a reporter that is size excluded from re-compartmentalization following nuclear rupture events. This allows for robust detection of factors influencing nuclear integrity in fixed cells. We combined this with an automated image analysis pipeline in a high-content siRNA screen to identify new proteins that both increase and decrease nuclear rupture frequency in cancer cells. Pathway analysis identified an enrichment of nuclear membrane and ER factors in our hits and we demonstrate that one of these, the protein phosphatase CTDNEP1, is required for nuclear stability. Further analysis of known rupture contributors, including a newly developed automated quantitative analysis of nuclear lamina gaps, strongly suggests that CTDNEP1 acts in a new pathway. Our findings provide new insights into the molecular mechanism of nuclear rupture and define a highly adaptable program for rupture analysis that removes a substantial barrier to new discoveries in the field. |
format | Online Article Text |
id | pubmed-10312541 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Cold Spring Harbor Laboratory |
record_format | MEDLINE/PubMed |
spelling | pubmed-103125412023-07-01 A high-content screen reveals new regulators of nuclear membrane stability Gunn, Amanda L. Yashchenko, Artem I. Dubrulle, Julien Johnson, Jodiene Hatch, Emily M. bioRxiv Article Nuclear membrane rupture is a physiological response to multiple in vivo processes, such as cell migration, that can cause extensive genome instability and upregulate invasive and inflammatory pathways. However, the underlying molecular mechanisms of rupture are unclear and few regulators have been identified. In this study, we developed a reporter that is size excluded from re-compartmentalization following nuclear rupture events. This allows for robust detection of factors influencing nuclear integrity in fixed cells. We combined this with an automated image analysis pipeline in a high-content siRNA screen to identify new proteins that both increase and decrease nuclear rupture frequency in cancer cells. Pathway analysis identified an enrichment of nuclear membrane and ER factors in our hits and we demonstrate that one of these, the protein phosphatase CTDNEP1, is required for nuclear stability. Further analysis of known rupture contributors, including a newly developed automated quantitative analysis of nuclear lamina gaps, strongly suggests that CTDNEP1 acts in a new pathway. Our findings provide new insights into the molecular mechanism of nuclear rupture and define a highly adaptable program for rupture analysis that removes a substantial barrier to new discoveries in the field. Cold Spring Harbor Laboratory 2023-09-10 /pmc/articles/PMC10312541/ /pubmed/37398267 http://dx.doi.org/10.1101/2023.05.30.542944 Text en https://creativecommons.org/licenses/by-nc-nd/4.0/This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License (https://creativecommons.org/licenses/by-nc-nd/4.0/) , which allows reusers to copy and distribute the material in any medium or format in unadapted form only, for noncommercial purposes only, and only so long as attribution is given to the creator. |
spellingShingle | Article Gunn, Amanda L. Yashchenko, Artem I. Dubrulle, Julien Johnson, Jodiene Hatch, Emily M. A high-content screen reveals new regulators of nuclear membrane stability |
title | A high-content screen reveals new regulators of nuclear membrane stability |
title_full | A high-content screen reveals new regulators of nuclear membrane stability |
title_fullStr | A high-content screen reveals new regulators of nuclear membrane stability |
title_full_unstemmed | A high-content screen reveals new regulators of nuclear membrane stability |
title_short | A high-content screen reveals new regulators of nuclear membrane stability |
title_sort | high-content screen reveals new regulators of nuclear membrane stability |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10312541/ https://www.ncbi.nlm.nih.gov/pubmed/37398267 http://dx.doi.org/10.1101/2023.05.30.542944 |
work_keys_str_mv | AT gunnamandal ahighcontentscreenrevealsnewregulatorsofnuclearmembranestability AT yashchenkoartemi ahighcontentscreenrevealsnewregulatorsofnuclearmembranestability AT dubrullejulien ahighcontentscreenrevealsnewregulatorsofnuclearmembranestability AT johnsonjodiene ahighcontentscreenrevealsnewregulatorsofnuclearmembranestability AT hatchemilym ahighcontentscreenrevealsnewregulatorsofnuclearmembranestability AT gunnamandal highcontentscreenrevealsnewregulatorsofnuclearmembranestability AT yashchenkoartemi highcontentscreenrevealsnewregulatorsofnuclearmembranestability AT dubrullejulien highcontentscreenrevealsnewregulatorsofnuclearmembranestability AT johnsonjodiene highcontentscreenrevealsnewregulatorsofnuclearmembranestability AT hatchemilym highcontentscreenrevealsnewregulatorsofnuclearmembranestability |