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Structure and Function of SET and MYND Domain-Containing Proteins
SET (Suppressor of variegation, Enhancer of Zeste, Trithorax) and MYND (Myeloid-Nervy-DEAF1) domain-containing proteins (SMYD) have been found to methylate a variety of histone and non-histone targets which contribute to their various roles in cell regulation including chromatin remodeling, transcri...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4307310/ https://www.ncbi.nlm.nih.gov/pubmed/25580534 http://dx.doi.org/10.3390/ijms16011406 |
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author | Spellmon, Nicholas Holcomb, Joshua Trescott, Laura Sirinupong, Nualpun Yang, Zhe |
author_facet | Spellmon, Nicholas Holcomb, Joshua Trescott, Laura Sirinupong, Nualpun Yang, Zhe |
author_sort | Spellmon, Nicholas |
collection | PubMed |
description | SET (Suppressor of variegation, Enhancer of Zeste, Trithorax) and MYND (Myeloid-Nervy-DEAF1) domain-containing proteins (SMYD) have been found to methylate a variety of histone and non-histone targets which contribute to their various roles in cell regulation including chromatin remodeling, transcription, signal transduction, and cell cycle control. During early development, SMYD proteins are believed to act as an epigenetic regulator for myogenesis and cardiomyocyte differentiation as they are abundantly expressed in cardiac and skeletal muscle. SMYD proteins are also of therapeutic interest due to the growing list of carcinomas and cardiovascular diseases linked to SMYD overexpression or dysfunction making them a putative target for drug intervention. This review will examine the biological relevance and gather all of the current structural data of SMYD proteins. |
format | Online Article Text |
id | pubmed-4307310 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-43073102015-02-02 Structure and Function of SET and MYND Domain-Containing Proteins Spellmon, Nicholas Holcomb, Joshua Trescott, Laura Sirinupong, Nualpun Yang, Zhe Int J Mol Sci Review SET (Suppressor of variegation, Enhancer of Zeste, Trithorax) and MYND (Myeloid-Nervy-DEAF1) domain-containing proteins (SMYD) have been found to methylate a variety of histone and non-histone targets which contribute to their various roles in cell regulation including chromatin remodeling, transcription, signal transduction, and cell cycle control. During early development, SMYD proteins are believed to act as an epigenetic regulator for myogenesis and cardiomyocyte differentiation as they are abundantly expressed in cardiac and skeletal muscle. SMYD proteins are also of therapeutic interest due to the growing list of carcinomas and cardiovascular diseases linked to SMYD overexpression or dysfunction making them a putative target for drug intervention. This review will examine the biological relevance and gather all of the current structural data of SMYD proteins. MDPI 2015-01-08 /pmc/articles/PMC4307310/ /pubmed/25580534 http://dx.doi.org/10.3390/ijms16011406 Text en © 2015 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 license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Spellmon, Nicholas Holcomb, Joshua Trescott, Laura Sirinupong, Nualpun Yang, Zhe Structure and Function of SET and MYND Domain-Containing Proteins |
title | Structure and Function of SET and MYND Domain-Containing Proteins |
title_full | Structure and Function of SET and MYND Domain-Containing Proteins |
title_fullStr | Structure and Function of SET and MYND Domain-Containing Proteins |
title_full_unstemmed | Structure and Function of SET and MYND Domain-Containing Proteins |
title_short | Structure and Function of SET and MYND Domain-Containing Proteins |
title_sort | structure and function of set and mynd domain-containing proteins |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4307310/ https://www.ncbi.nlm.nih.gov/pubmed/25580534 http://dx.doi.org/10.3390/ijms16011406 |
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