TY - JOUR
T1 - Myosin heavy chain is stabilized by BCL-2 interacting cell death suppressor (BIS) in skeletal muscle
AU - Hong, Jin
AU - Park, Jun Sub
AU - Lee, Hyun
AU - Jeong, Jaemin
AU - Yun, Hye Hyeon
AU - Kim, Hye Yun
AU - Ko, Young Gyu
AU - Lee, Jeong Hwa
N1 - Funding Information:
This research was supported by the Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the minister of Education, Science and Technology (2011-001752, 2015R1A5A1009024 and 2012R1A1A2007589). Author contributions: YGK and JHL developed the concept of the research, interpreted the results and edited the manuscript. JH, JSP, HL, JMJ, HYK and HHY performed the experiments. JH also contributed to the drafting of the manuscript.
Publisher Copyright:
© 2016 KSBMB. All rights reserved.
PY - 2016/4
Y1 - 2016/4
N2 - BCL-2 interacting cell death suppressor (BIS), which is ubiquitously expressed, has important roles in various cellular processes, such as apoptosis, the cellular stress response, migration and invasion and protein quality control. In particular, BIS is highly expressed in skeletal and cardiac muscles, and BIS gene mutations result in human myopathy. In this study, we show that mRNA and protein levels of BIS were markedly increased during skeletal myogenesis in C2C12 cells and mouse satellite cells. BIS knockdown did not prevent the early stage of skeletal myogenesis, but did induce muscle atrophy and a decrease in the diameter of myotubes. BIS knockdown significantly suppressed the expression level of myosin heavy chain (MyHC) without changing the expression levels of myogenic marker proteins, such as Mgn, Cav-3 and MG53. In addition, BIS endogenously interacted with MyHC, and BIS knockdown induced MyHC ubiquitination and degradation. From these data, we conclude that molecular association of MyHC and BIS is necessary for MyHC stabilization in skeletal muscle.
AB - BCL-2 interacting cell death suppressor (BIS), which is ubiquitously expressed, has important roles in various cellular processes, such as apoptosis, the cellular stress response, migration and invasion and protein quality control. In particular, BIS is highly expressed in skeletal and cardiac muscles, and BIS gene mutations result in human myopathy. In this study, we show that mRNA and protein levels of BIS were markedly increased during skeletal myogenesis in C2C12 cells and mouse satellite cells. BIS knockdown did not prevent the early stage of skeletal myogenesis, but did induce muscle atrophy and a decrease in the diameter of myotubes. BIS knockdown significantly suppressed the expression level of myosin heavy chain (MyHC) without changing the expression levels of myogenic marker proteins, such as Mgn, Cav-3 and MG53. In addition, BIS endogenously interacted with MyHC, and BIS knockdown induced MyHC ubiquitination and degradation. From these data, we conclude that molecular association of MyHC and BIS is necessary for MyHC stabilization in skeletal muscle.
UR - http://www.scopus.com/inward/record.url?scp=85016641550&partnerID=8YFLogxK
U2 - 10.1038/EMM.2016.2
DO - 10.1038/EMM.2016.2
M3 - Article
C2 - 27034027
AN - SCOPUS:85016641550
SN - 1226-3613
VL - 48
JO - Experimental and Molecular Medicine
JF - Experimental and Molecular Medicine
IS - 4
M1 - e225
ER -