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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...

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Autores principales: Spellmon, Nicholas, Holcomb, Joshua, Trescott, Laura, Sirinupong, Nualpun, Yang, Zhe
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2015
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.
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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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