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Myosin heavy chain is stabilized by BCL-2 interacting cell death suppressor (BIS) in skeletal muscle

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 muscl...

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Autores principales: Hong, Jin, Park, Jun-Sub, Lee, Hyun, Jeong, Jaemin, Hyeon Yun, Hye, Yun Kim, Hye, Ko, Young-Gyu, Lee, Jeong-Hwa
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4855277/
https://www.ncbi.nlm.nih.gov/pubmed/27034027
http://dx.doi.org/10.1038/emm.2016.2
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author Hong, Jin
Park, Jun-Sub
Lee, Hyun
Jeong, Jaemin
Hyeon Yun, Hye
Yun Kim, Hye
Ko, Young-Gyu
Lee, Jeong-Hwa
author_facet Hong, Jin
Park, Jun-Sub
Lee, Hyun
Jeong, Jaemin
Hyeon Yun, Hye
Yun Kim, Hye
Ko, Young-Gyu
Lee, Jeong-Hwa
author_sort Hong, Jin
collection PubMed
description 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.
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spelling pubmed-48552772016-05-18 Myosin heavy chain is stabilized by BCL-2 interacting cell death suppressor (BIS) in skeletal muscle Hong, Jin Park, Jun-Sub Lee, Hyun Jeong, Jaemin Hyeon Yun, Hye Yun Kim, Hye Ko, Young-Gyu Lee, Jeong-Hwa Exp Mol Med Original Article 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. Nature Publishing Group 2016-04 2016-04-01 /pmc/articles/PMC4855277/ /pubmed/27034027 http://dx.doi.org/10.1038/emm.2016.2 Text en Copyright © 2016 KSBMB. http://creativecommons.org/licenses/by-nc-nd/4.0/ This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/4.0/
spellingShingle Original Article
Hong, Jin
Park, Jun-Sub
Lee, Hyun
Jeong, Jaemin
Hyeon Yun, Hye
Yun Kim, Hye
Ko, Young-Gyu
Lee, Jeong-Hwa
Myosin heavy chain is stabilized by BCL-2 interacting cell death suppressor (BIS) in skeletal muscle
title Myosin heavy chain is stabilized by BCL-2 interacting cell death suppressor (BIS) in skeletal muscle
title_full Myosin heavy chain is stabilized by BCL-2 interacting cell death suppressor (BIS) in skeletal muscle
title_fullStr Myosin heavy chain is stabilized by BCL-2 interacting cell death suppressor (BIS) in skeletal muscle
title_full_unstemmed Myosin heavy chain is stabilized by BCL-2 interacting cell death suppressor (BIS) in skeletal muscle
title_short Myosin heavy chain is stabilized by BCL-2 interacting cell death suppressor (BIS) in skeletal muscle
title_sort myosin heavy chain is stabilized by bcl-2 interacting cell death suppressor (bis) in skeletal muscle
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4855277/
https://www.ncbi.nlm.nih.gov/pubmed/27034027
http://dx.doi.org/10.1038/emm.2016.2
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