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The rod domain is not essential for the function of plectin in maintaining tissue integrity

Epidermolysis bullosa simplex associated with late-onset muscular dystrophy (EBS-MD) is an autosomal recessive disorder resulting from mutations in the plectin gene. The majority of these mutations occur within the large exon 31 encoding the central rod domain and leave the production of a low-level...

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Autores principales: Ketema, Mirjam, Secades, Pablo, Kreft, Maaike, Nahidiazar, Leila, Janssen, Hans, Jalink, Kees, de Pereda, Jose M., Sonnenberg, Arnoud
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4571296/
https://www.ncbi.nlm.nih.gov/pubmed/25971800
http://dx.doi.org/10.1091/mbc.E15-01-0043
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author Ketema, Mirjam
Secades, Pablo
Kreft, Maaike
Nahidiazar, Leila
Janssen, Hans
Jalink, Kees
de Pereda, Jose M.
Sonnenberg, Arnoud
author_facet Ketema, Mirjam
Secades, Pablo
Kreft, Maaike
Nahidiazar, Leila
Janssen, Hans
Jalink, Kees
de Pereda, Jose M.
Sonnenberg, Arnoud
author_sort Ketema, Mirjam
collection PubMed
description Epidermolysis bullosa simplex associated with late-onset muscular dystrophy (EBS-MD) is an autosomal recessive disorder resulting from mutations in the plectin gene. The majority of these mutations occur within the large exon 31 encoding the central rod domain and leave the production of a low-level rodless plectin splice variant unaffected. To investigate the function of the rod domain, we generated rodless plectin mice through conditional deletion of exon 31. Rodless plectin mice develop normally without signs of skin blistering or muscular dystrophy. Plectin localization and hemidesmosome organization are unaffected in rodless plectin mice. However, superresolution microscopy revealed a closer juxtaposition of the C-terminus of plectin to the integrin β4 subunit in rodless plectin keratinocytes. Wound healing occurred slightly faster in rodless plectin mice than in wild-type mice, and keratinocytes migration was increased in the absence of the rod domain. The faster migration of rodless plectin keratinocytes is not due to altered biochemical properties because, like full-length plectin, rodless plectin is a dimeric protein. Our data demonstrate that rodless plectin can functionally compensate for the loss of full-length plectin in mice. Thus the low expression level of plectin rather than the absence of the rod domain dictates the development of EBS-MD.
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spelling pubmed-45712962015-09-29 The rod domain is not essential for the function of plectin in maintaining tissue integrity Ketema, Mirjam Secades, Pablo Kreft, Maaike Nahidiazar, Leila Janssen, Hans Jalink, Kees de Pereda, Jose M. Sonnenberg, Arnoud Mol Biol Cell Articles Epidermolysis bullosa simplex associated with late-onset muscular dystrophy (EBS-MD) is an autosomal recessive disorder resulting from mutations in the plectin gene. The majority of these mutations occur within the large exon 31 encoding the central rod domain and leave the production of a low-level rodless plectin splice variant unaffected. To investigate the function of the rod domain, we generated rodless plectin mice through conditional deletion of exon 31. Rodless plectin mice develop normally without signs of skin blistering or muscular dystrophy. Plectin localization and hemidesmosome organization are unaffected in rodless plectin mice. However, superresolution microscopy revealed a closer juxtaposition of the C-terminus of plectin to the integrin β4 subunit in rodless plectin keratinocytes. Wound healing occurred slightly faster in rodless plectin mice than in wild-type mice, and keratinocytes migration was increased in the absence of the rod domain. The faster migration of rodless plectin keratinocytes is not due to altered biochemical properties because, like full-length plectin, rodless plectin is a dimeric protein. Our data demonstrate that rodless plectin can functionally compensate for the loss of full-length plectin in mice. Thus the low expression level of plectin rather than the absence of the rod domain dictates the development of EBS-MD. The American Society for Cell Biology 2015-07-01 /pmc/articles/PMC4571296/ /pubmed/25971800 http://dx.doi.org/10.1091/mbc.E15-01-0043 Text en © 2015 Ketema et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology.
spellingShingle Articles
Ketema, Mirjam
Secades, Pablo
Kreft, Maaike
Nahidiazar, Leila
Janssen, Hans
Jalink, Kees
de Pereda, Jose M.
Sonnenberg, Arnoud
The rod domain is not essential for the function of plectin in maintaining tissue integrity
title The rod domain is not essential for the function of plectin in maintaining tissue integrity
title_full The rod domain is not essential for the function of plectin in maintaining tissue integrity
title_fullStr The rod domain is not essential for the function of plectin in maintaining tissue integrity
title_full_unstemmed The rod domain is not essential for the function of plectin in maintaining tissue integrity
title_short The rod domain is not essential for the function of plectin in maintaining tissue integrity
title_sort rod domain is not essential for the function of plectin in maintaining tissue integrity
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4571296/
https://www.ncbi.nlm.nih.gov/pubmed/25971800
http://dx.doi.org/10.1091/mbc.E15-01-0043
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