Stabilin-2 modulates the efficiency of myoblast fusion during myogenic differentiation and muscle regeneration

Seung-Yoon Park (), Youngeun Yun, Jung-Suk Lim, Mi-Jin Kim, Sang-Yeob Kim, Jung-Eun Kim and In-San Kim ()
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Seung-Yoon Park: School of Medicine, Dongguk University
Youngeun Yun: School of Medicine, Kyungpook National University
Jung-Suk Lim: School of Medicine, Dongguk University
Mi-Jin Kim: School of Medicine, Dongguk University
Sang-Yeob Kim: University of Ulsan, College of Medicine & Asan Institute for Life Sciences, Asan Medical Center
Jung-Eun Kim: School of Medicine, Kyungpook National University
In-San Kim: Biomedical Research Institute, Korea Institute Science and Technology

Nature Communications, 2016, vol. 7, issue 1, 1-15

Abstract: Abstract Myoblast fusion is essential for the formation of skeletal muscle myofibres. Studies have shown that phosphatidylserine is necessary for myoblast fusion, but the underlying mechanism is not known. Here we show that the phosphatidylserine receptor stabilin-2 acts as a membrane protein for myoblast fusion during myogenic differentiation and muscle regeneration. Stabilin-2 expression is induced during myogenic differentiation, and is regulated by calcineurin/NFAT signalling in myoblasts. Forced expression of stabilin-2 in myoblasts is associated with increased myotube formation, whereas deficiency of stabilin-2 results in the formation of small, thin myotubes. Stab2-deficient mice have myofibres with small cross-sectional area and few myonuclei and impaired muscle regeneration after injury. Importantly, myoblasts lacking stabilin-2 have reduced phosphatidylserine-dependent fusion. Collectively, our results show that stabilin-2 contributes to phosphatidylserine-dependent myoblast fusion and provide new insights into the molecular mechanism by which phosphatidylserine mediates myoblast fusion during muscle growth and regeneration.

Date: 2016
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DOI: 10.1038/ncomms10871

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