Rui Xu
Shaojun Du
aDepartment of Biochemistry and Molecular Biology, Institute of Marine and Environmental Technology, University of Maryland School of Medicine, Baltimore, MD 21202, USA
bKey Laboratory of Experimental Marine Biology, Center for Ocean Mega-Science, Institute of Oceanology, Chinese Academy of Sciences, Qingdao 266071, China
More InformationCorresponding author: E-mail address: sdu@som.umaryland.edu (Shaojun Du)
Received Date: 2020-10-29
Accepted Date:2021-03-02
Rev Recd Date:2021-02-22
Available Online: 2021-04-07 Publish Date:2021-03-20
Abstract
Abstract
Skeletal and cardiac muscles are striated myofibers that contain highly organized sarcomeres for muscle contraction. Recent studies revealed that Smyd1, a lysine methyltransferase, plays a key role in sarcomere assembly in heart and trunk skeletal muscles. However, Smyd1 expression and function in craniofacial muscles are not known. Here, we analyze the developmental expression and function of two smyd1 paralogous genes, smyd1a and smyd1b, in craniofacial and cardiac muscles of zebrafish embryos. Our data show that loss of smyd1a (smyd1a) or smyd1b (smyd1b) has no visible effects on myogenic commitment and expression of myod and myosin heavy-chain mRNA transcripts in craniofacial muscles. However, myosin heavy-chain protein accumulation and sarcomere organization are dramatically reduced in smyd1b single mutant, and almost completely diminish in smyd1a; smyd1b double mutant, but not in smyd1a mutant. Similar defects are also observed in cardiac muscles ofsmyd1b mutant. Defective craniofacial and cardiac muscle formation is associated with an upregulation of hsp90α1 and unc45b mRNA expression in smyd1b and smyd1a; smyd1b mutants. Together, our studies indicate that Smyd1b, but not Smyd1a, plays a key role in myosin heavy-chain protein expression and sarcomere organization in craniofacial and cardiac muscles. Loss of smyd1b results in muscle-specific stress response.Keywords: Smyd1,
Myosin,
Sarcomere,
Craniofacial muscle,
Cardiac muscle
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