PCAF Involvement in Lamin A/C-HDAC2 Interplay during the Early Phase of Muscle Differentiation.

Cells
Spartaco SantiElisabetta Mattioli

Abstract

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 lamina 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 molecul...Continue Reading

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Citations

Mar 29, 2021·Current Opinion in Genetics & Development·Victoria E HoskinsKaren L Reddy
May 1, 2021·International Journal of Molecular Sciences·Lorenzo MaggiGiovanna Lattanzi
Jun 12, 2021·Epigenetics & Chromatin·Ying-Jiun C Chen, Sharon Y R Dent
Jun 22, 2021·Trends in Biochemical Sciences·Laura A Murray-Nerger, Ileana M Cristea

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Methods Mentioned

BETA
acetylation
histone acetylation
transfection
proximity ligation assay
co-immunoprecipitation

Software Mentioned

Photoshop
Elements
Duolink Image Tool
Elements Advanced Research
NIS
NIS Elements Advanced Research
NIS Elements AR

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