MYSM1 attenuates osteoarthritis by recruiting PP2A to deubiquitinate and dephosphorylate RIPK2

Bone Res. 2025 Jan 2;13(1):3. doi: 10.1038/s41413-024-00368-y.

Abstract

Osteoarthritis (OA), the most prevalent degenerative joint disease, is marked by cartilage degradation and pathological alterations in surrounding tissues. Currently, no effective disease-modifying treatments exist. This study aimed to elucidate the critical roles of Myb-like, SWIRM, and MPN domains 1 (MYSM1) and its downstream effector, Receptor-interacting protein kinase 2 (RIPK2), in OA pathogenesis and the underlying mechanisms. Our findings revealed reduced MYSM1 levels in the cartilage of OA patients and mouse models. Genetic or adenovirus-induced MYSM1 knockout exacerbated OA progression in mice, whereas MYSM1 overexpression mitigated it. Mechanistically, MYSM1 inhibited the NF-κB and MAPK signaling pathways. Conversely, downstream RIPK2 significantly increased OA-like phenotypes and activated the NF-κB and MAPK pathways. The Ripk2S176D mutation accelerated OA pathogenesis, while Ripk2 silencing or Ripk2S176A mutation deactivated NF-κB and MAPK pathways, counteracting the role of MYSM1. MYSM1 deubiquitinates and dephosphorylates RIPK2S176 by recruiting protein phosphatase 2 A (PP2A). These results suggest that targeting MYSM1 or downstream RIPK2 offers promising therapeutic potential for OA.

MeSH terms

  • Animals
  • Humans
  • Male
  • Mice
  • Mice, Inbred C57BL
  • Mice, Knockout
  • NF-kappa B / metabolism
  • Osteoarthritis* / genetics
  • Osteoarthritis* / metabolism
  • Osteoarthritis* / pathology
  • Phosphorylation
  • Protein Phosphatase 2* / genetics
  • Protein Phosphatase 2* / metabolism
  • Receptor-Interacting Protein Serine-Threonine Kinase 2* / genetics
  • Receptor-Interacting Protein Serine-Threonine Kinase 2* / metabolism
  • Ubiquitination*

Substances

  • Receptor-Interacting Protein Serine-Threonine Kinase 2
  • Protein Phosphatase 2
  • NF-kappa B
  • RIPK2 protein, human