Jiale Yu

Wenzhou Medical University

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Hongshan Ge

Taizhou People's Hospital

Shiyuan Huang

Huazhong University of Science and Technology

Xiaona Wang

Second Affiliated Hospital & Yuying Children's Hospital of Wenzhou Medical University

Yang Chen

Wenzhou Medical University

Chenkai Yang

Shanghai First People's Hospital

Huasong Huang

Sichuan University

Jun Pan

Second Affiliated Hospital & Yuying Children's Hospital of Wenzhou Medical University

Yifan Wu

Wenzhou Medical University

Hua Chen

Guangxi Normal University

Xiaodiao Kang

Second Affiliated Hospital & Yuying Children's Hospital of Wenzhou Medical University

Cooperative Institutions

Wenzhou Medical University

Second Affiliated Hospital & Yuying Children's Hospital of Wenzhou Medical University

Nanjing Medical University

Chinese Academy of Medical Sciences & Peking Union Medical College

Nantong University

Dalian Medical University

Sichuan University

Shanghai Jiao Tong University

Peking Union Medical College Hospital

Army Medical University

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The protective effect of sophocarpine in osteoarthritis: An in vitro and in vivo study

International Immunopharmacology (2018)

Yifan Wu Xingyu Zhu Xiaodiao Kang Huasong Huang Jiale Yu

Proinflammatory cytokine

Aggrecan

10.1016/j.intimp.2018.11.046

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Citations (13)

Yap regulates mitochondrial structural remodeling during myoblast differentiation

AJP Cell Physiology (2018)

Shiyuan Huang Xiaona Wang Xinmei Wu Jiale Yu JinJing Li

Yes-associated protein (Yap) is a core transcriptional coactivator in the downstream Hippo pathway that regulates cell proliferation and tissue growth. However, its role in the regulation of myoblast differentiation remains unclear. Regulation of mitochondrial networks by dynamin-related protein 1 (Drp1) and mitofusion 2 (Mfn2) is crucial for the activation of myoblast differentiation. In the present study, we investigated the interplay between the Hippo/Yap pathway and protein contents of Mfn2 and Drp1 during myoblast differentiation. The Hippo/Yap pathway was inactivated at the early stage of myoblast differentiation due to the decreased ratio of phosphorylated mammalian sterile 20 kinases 1/2 (p-Mst1/2) to Mst1/2, phosphorylated large tumor suppressor 1 (p-Lats1) to Lats1, and phosphorylated Yap (serine 112, p-Yap S112) to Yap, which resulted in the translocation of Yap from cytoplasm to nucleus, increased protein content of Drp1, and mitochondrial fission events. Downregulation of Yap inhibited myoblast differentiation and decreased the content of Drp1, which resulted in elongated mitochondria, fused mitochondrial networks, and collapsed mitochondrial membrane potential. Together, our data indicate that inactivation of the Hippo/Yap pathway could induce mitochondrial fission by promoting Drp1 content at the early stage of myoblast differentiation.

Hippo signaling pathway

MFN2

10.1152/ajpcell.00112.2018

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LonP1 regulates mitochondrial network remodeling through the PINK1/Parkin pathway during myoblast differentiation

AJP Cell Physiology (2020)

Shiyuan Huang Xiaona Wang Jiale Yu Yu Tian Chenkai Yang

Myoblast differentiation is a crucial process for myogenesis. Mitochondria function as an energy-providing machine that is critical to this process, and mitochondrial dysfunction can prevent myoblasts from fusing into myotubes. However, the molecular mechanisms underlying the dynamic regulation of mitochondrial networks remain poorly understood. In the present study, we found that the PTEN induced kinase 1 (PINK1)/Parkin (an E3 ubiquitin-protein ligase) pathway is activated at the early stage of myoblast differentiation. Moreover, downregulation of mitofusin 2 (Mfn2) and increased dynamin-related protein 1 (Drp1) resulted in loosely formed mitochondria during this period. Furthermore, selective knockdown of the mitochondrial matrix protein Lon peptidase-1 (LonP1) at the early stage of myoblast differentiation induced mitochondrial depolarization and suppressed the PINK1/Parkin pathway and reduced Mfn2 and Drp1 levels, which blocked mitochondrial remodeling and myoblast differentiation. Overall, these data demonstrate that LonP1 promotes myoblast differentiation by regulating PINK1/Parkin-mediated mitochondrial remodeling.

PINK1

MFN2

C2C12

10.1152/ajpcell.00589.2019

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LonP1 regulates mitochondrial network remodeling through the PINK1/Parkin pathway during myoblast differentiation (Supplementary Table-1.docx)

Figshare (2020)

Shiyuan Huang Xiaona Wang Hua Chen Jiale Yu Yu Tian

Myoblast differentiation is a crucial process for myogenesis. Mitochondria function as an energy-providing machine that is critical to this process, and mitochondrial dysfunction can prevent myoblasts from fusing into myotubes. However, the molecular mechanisms underlying the dynamic regulation of mitochondrial networks remain poorly understood. In the present study, we found that the PTEN induced kinase 1(PINK1) /Parkin (an E3 ubiquitin-protein ligase) pathway is activated at the early stage of myoblast differentiation. Moreover, downregulation of mitofusin 2 (Mfn2) and increased dynamin-related protein 1 (Drp1) resulted in loosely formed mitochondria during this period. Furthermore, selective knockdown of the mitochondrial matrix protein Lon proteinase-1 (LonP1) at the early stage of myoblast differentiation induced mitochondrial depolarization and suppressed the PINK1/Parkin pathway and reduced Mfn2 and Drp1 levels, which blocked mitochondrial remodeling and myoblast differentiation. Overall, these data suggest that LonP1 plays an essential role in maintaining the normal myoblast differentiation process, which partly by regulating PINK1/Parkin mediated mitochondrial remodeling.

PINK1

Table (database)

10.6084/m9.figshare.12715418

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