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Int. J. Mol. Sci. 2015, 16(1), 1406-1428; doi:10.3390/ijms16011406

Structure and Function of SET and MYND Domain-Containing Proteins

1
Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, 540 East Canfield Street, Detroit, MI 48201, USA
2
Nutraceuticals and Functional Food Research and Development Center, Prince of Songkla University, Hat-Yai, Songkhla 90112, Thailand
*
Author to whom correspondence should be addressed.
Academic Editor: Charles A. Collyer
Received: 5 December 2014 / Accepted: 5 January 2015 / Published: 8 January 2015
(This article belongs to the Special Issue Protein Crystallography in Molecular Biology 2015)
View Full-Text   |   Download PDF [12506 KB, uploaded 8 January 2015]   |  

Abstract

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. View Full-Text
Keywords: SMYD (SET and MYND domain-containing proteins); structure and function; SET (Suppressor of variegation, Enhancer of Zeste, Trithorax); MYND (Myeloid-Nervy-DEAF1) SMYD (SET and MYND domain-containing proteins); structure and function; SET (Suppressor of variegation, Enhancer of Zeste, Trithorax); MYND (Myeloid-Nervy-DEAF1)
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Spellmon, N.; Holcomb, J.; Trescott, L.; Sirinupong, N.; Yang, Z. Structure and Function of SET and MYND Domain-Containing Proteins. Int. J. Mol. Sci. 2015, 16, 1406-1428.

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