Lamin A/C mutants disturb sumo1 localization and sumoylation in vitro and in vivo.
A-type lamins A and C are nuclear intermediate filament proteins in which mutations have been implicated in multiple disease phenotypes commonly known as laminopathies. A few studies have implicated sumoylation in the regulation of A-type lamins. Sumoylation is a post-translational protein modificat...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2012-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3448699?pdf=render |
| _version_ | 1818416129278738432 |
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| author | Émilie Boudreau Sarah Labib Anne T Bertrand Valérie Decostre Pierrette M Bolongo Nicolas Sylvius Gisèle Bonne Frédérique Tesson |
| author_facet | Émilie Boudreau Sarah Labib Anne T Bertrand Valérie Decostre Pierrette M Bolongo Nicolas Sylvius Gisèle Bonne Frédérique Tesson |
| author_sort | Émilie Boudreau |
| collection | DOAJ |
| description | A-type lamins A and C are nuclear intermediate filament proteins in which mutations have been implicated in multiple disease phenotypes commonly known as laminopathies. A few studies have implicated sumoylation in the regulation of A-type lamins. Sumoylation is a post-translational protein modification that regulates a wide range of cellular processes through the attachment of small ubiquitin-related modifier (sumo) to various substrates. Here we showed that laminopathy mutants result in the mislocalization of sumo1 both in vitro (C2C12 cells overexpressing mutant lamins A and C) and in vivo (primary myoblasts and myopathic muscle tissue from the Lmna(H222P/H222P) mouse model). In C2C12 cells, we showed that the trapping of sumo1 in p.Asp192Gly, p.Gln353Lys, and p.Arg386Lys aggregates of lamin A/C correlated with an increased steady-state level of sumoylation. However, lamin A and C did not appear to be modified by sumo1. Our results suggest that mutant lamin A/C alters the dynamics of sumo1 and thus misregulation of sumoylation may be contributing to disease progression in laminopathies. |
| first_indexed | 2024-12-14T11:45:59Z |
| format | Article |
| id | doaj.art-065ff59cf9bf4d12bf4d1f3357baf172 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-14T11:45:59Z |
| publishDate | 2012-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-065ff59cf9bf4d12bf4d1f3357baf1722022-12-21T23:02:34ZengPublic Library of Science (PLoS)PLoS ONE1932-62032012-01-0179e4591810.1371/journal.pone.0045918Lamin A/C mutants disturb sumo1 localization and sumoylation in vitro and in vivo.Émilie BoudreauSarah LabibAnne T BertrandValérie DecostrePierrette M BolongoNicolas SylviusGisèle BonneFrédérique TessonA-type lamins A and C are nuclear intermediate filament proteins in which mutations have been implicated in multiple disease phenotypes commonly known as laminopathies. A few studies have implicated sumoylation in the regulation of A-type lamins. Sumoylation is a post-translational protein modification that regulates a wide range of cellular processes through the attachment of small ubiquitin-related modifier (sumo) to various substrates. Here we showed that laminopathy mutants result in the mislocalization of sumo1 both in vitro (C2C12 cells overexpressing mutant lamins A and C) and in vivo (primary myoblasts and myopathic muscle tissue from the Lmna(H222P/H222P) mouse model). In C2C12 cells, we showed that the trapping of sumo1 in p.Asp192Gly, p.Gln353Lys, and p.Arg386Lys aggregates of lamin A/C correlated with an increased steady-state level of sumoylation. However, lamin A and C did not appear to be modified by sumo1. Our results suggest that mutant lamin A/C alters the dynamics of sumo1 and thus misregulation of sumoylation may be contributing to disease progression in laminopathies.http://europepmc.org/articles/PMC3448699?pdf=render |
| spellingShingle | Émilie Boudreau Sarah Labib Anne T Bertrand Valérie Decostre Pierrette M Bolongo Nicolas Sylvius Gisèle Bonne Frédérique Tesson Lamin A/C mutants disturb sumo1 localization and sumoylation in vitro and in vivo. PLoS ONE |
| title | Lamin A/C mutants disturb sumo1 localization and sumoylation in vitro and in vivo. |
| title_full | Lamin A/C mutants disturb sumo1 localization and sumoylation in vitro and in vivo. |
| title_fullStr | Lamin A/C mutants disturb sumo1 localization and sumoylation in vitro and in vivo. |
| title_full_unstemmed | Lamin A/C mutants disturb sumo1 localization and sumoylation in vitro and in vivo. |
| title_short | Lamin A/C mutants disturb sumo1 localization and sumoylation in vitro and in vivo. |
| title_sort | lamin a c mutants disturb sumo1 localization and sumoylation in vitro and in vivo |
| url | http://europepmc.org/articles/PMC3448699?pdf=render |
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