6533b82afe1ef96bd128b7c4
RESEARCH PRODUCT
Interaction between ROR1 and MuSK activation complex in myogenic cells
Katja SummalaDaniela UngureanuHarlan BarkerHanna KarvonenWilhelmiina Niininensubject
0301 basic medicineSatellite Cells Skeletal MuscleBiophysicsMuscle ProteinsReceptor Tyrosine Kinase-like Orphan ReceptorsBiochemistryReceptor tyrosine kinaseCell LineProinflammatory cytokineMice03 medical and health sciencesProtein DomainsStructural BiologyChlorocebus aethiopsGeneticsAnimalsHumansReceptors CholinergicProtein phosphorylationPhosphorylationMolecular BiologyCell ProliferationBinding SitesbiologyKinaseChemistryActivator (genetics)Receptor Protein-Tyrosine KinasesCell DifferentiationROR2Cell BiologyCell biologyHEK293 Cells030104 developmental biologyCOS CellsROR1biology.proteinPhosphorylationProtein Bindingdescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2017-12-01 | FEBS Letters |