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PCAF Involvement in Lamin A/C-HDAC2 Interplay during the Early Phase of Muscle Differentiation
Lamin A/C has been implicated in the epigenetic regulation of muscle gene expression through dynamic interaction with chromatin domains and epigenetic enzymes. We previously showed that lamin A/C interacts with histone deacetylase 2 (HDAC2). In this study, we deepened the relevance and regulation of...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7409167/ https://www.ncbi.nlm.nih.gov/pubmed/32698523 http://dx.doi.org/10.3390/cells9071735 |
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author | Santi, Spartaco Cenni, Vittoria Capanni, Cristina Lattanzi, Giovanna Mattioli, Elisabetta |
author_facet | Santi, Spartaco Cenni, Vittoria Capanni, Cristina Lattanzi, Giovanna Mattioli, Elisabetta |
author_sort | Santi, Spartaco |
collection | PubMed |
description | Lamin A/C has been implicated in the epigenetic regulation of muscle gene expression through dynamic interaction with chromatin domains and epigenetic enzymes. We previously showed that lamin A/C interacts with histone deacetylase 2 (HDAC2). In this study, we deepened the relevance and regulation of lamin A/C-HDAC2 interaction in human muscle cells. We present evidence that HDAC2 binding to lamin A/C is related to HDAC2 acetylation on lysine 75 and expression of p300-CBP associated factor (PCAF), an acetyltransferase known to acetylate HDAC2. Our findings show that lamin A and farnesylated prelamin A promote PCAF recruitment to the nuclear lamina and lamin A/C binding in human myoblasts committed to myogenic differentiation, while protein interaction is decreased in differentiating myotubes. Interestingly, PCAF translocation to the nuclear envelope, as well as lamin A/C-PCAF interaction, are reduced by transient expression of lamin A mutated forms causing Emery Dreifuss muscular dystrophy. Consistent with this observation, lamin A/C interaction with both PCAF and HDAC2 is significantly reduced in Emery–Dreifuss muscular dystrophy myoblasts. Overall, these results support the view that, by recruiting PCAF and HDAC2 in a molecular platform, lamin A/C might contribute to regulate their epigenetic activity required in the early phase of muscle differentiation. |
format | Online Article Text |
id | pubmed-7409167 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-74091672020-08-26 PCAF Involvement in Lamin A/C-HDAC2 Interplay during the Early Phase of Muscle Differentiation Santi, Spartaco Cenni, Vittoria Capanni, Cristina Lattanzi, Giovanna Mattioli, Elisabetta Cells Article Lamin A/C has been implicated in the epigenetic regulation of muscle gene expression through dynamic interaction with chromatin domains and epigenetic enzymes. We previously showed that lamin A/C interacts with histone deacetylase 2 (HDAC2). In this study, we deepened the relevance and regulation of lamin A/C-HDAC2 interaction in human muscle cells. We present evidence that HDAC2 binding to lamin A/C is related to HDAC2 acetylation on lysine 75 and expression of p300-CBP associated factor (PCAF), an acetyltransferase known to acetylate HDAC2. Our findings show that lamin A and farnesylated prelamin A promote PCAF recruitment to the nuclear lamina and lamin A/C binding in human myoblasts committed to myogenic differentiation, while protein interaction is decreased in differentiating myotubes. Interestingly, PCAF translocation to the nuclear envelope, as well as lamin A/C-PCAF interaction, are reduced by transient expression of lamin A mutated forms causing Emery Dreifuss muscular dystrophy. Consistent with this observation, lamin A/C interaction with both PCAF and HDAC2 is significantly reduced in Emery–Dreifuss muscular dystrophy myoblasts. Overall, these results support the view that, by recruiting PCAF and HDAC2 in a molecular platform, lamin A/C might contribute to regulate their epigenetic activity required in the early phase of muscle differentiation. MDPI 2020-07-20 /pmc/articles/PMC7409167/ /pubmed/32698523 http://dx.doi.org/10.3390/cells9071735 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Santi, Spartaco Cenni, Vittoria Capanni, Cristina Lattanzi, Giovanna Mattioli, Elisabetta PCAF Involvement in Lamin A/C-HDAC2 Interplay during the Early Phase of Muscle Differentiation |
title | PCAF Involvement in Lamin A/C-HDAC2 Interplay during the Early Phase of Muscle Differentiation |
title_full | PCAF Involvement in Lamin A/C-HDAC2 Interplay during the Early Phase of Muscle Differentiation |
title_fullStr | PCAF Involvement in Lamin A/C-HDAC2 Interplay during the Early Phase of Muscle Differentiation |
title_full_unstemmed | PCAF Involvement in Lamin A/C-HDAC2 Interplay during the Early Phase of Muscle Differentiation |
title_short | PCAF Involvement in Lamin A/C-HDAC2 Interplay during the Early Phase of Muscle Differentiation |
title_sort | pcaf involvement in lamin a/c-hdac2 interplay during the early phase of muscle differentiation |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7409167/ https://www.ncbi.nlm.nih.gov/pubmed/32698523 http://dx.doi.org/10.3390/cells9071735 |
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