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FEBS Lett. 2018 Feb;592(3):434-445. doi: 10.1002/1873-3468.12966. Epub 2018 Jan 14.

Interaction between ROR1 and MuSK activation complex in myogenic cells.

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BioMediTech Institute, University of Tampere, Finland.
Faculty of Medicine and Life Sciences, University of Tampere, Finland.
Department of Biological and Environmental Science, University of Jyväskylä, Finland.


The ROR family of receptor tyrosine kinases, ROR1 and ROR2, is known to play an important role during skeletal muscle regeneration. ROR1 has a critical role in regulating satellite cell (SC) proliferation during muscle regeneration, and proinflammatory cytokines such as TNF-α and IL-1β can induce expression of ROR1 in myogenic cells via NF-κB activation. While searching for ROR1-interacting proteins in myogenic cells, we identified MuSK as a ROR1-binding protein. MuSK interacts with and phosphorylates ROR1 at the cytoplasmic proline-rich domain. ROR1 also interacts with the MuSK activator Dok-7 independently of MuSK interaction. Collectively, our results identified ROR1 as a new interacting partner for MuSK and Dok-7, which may have an important role in myogenic cell signaling.


C2C12 cells; kinases; muscle regeneration; myogenic differentiation; protein phosphorylation; protein-protein interaction

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