WWOX deficiency uncovers a cell-autonomous mechanism impairing myelin repair

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This study investigates how the WW domain–containing oxidoreductase WWOX regulates oligodendrocyte precursor (OPC) differentiation and remyelination, focusing on molecular programs governing myelin repair. By reanalyzing single-nucleus RNA sequencing from multiple sclerosis (MS) lesions and using conditional deletion of Wwox in oligodendroglia, the authors found that WWOX loss impaired OPC differentiation, increased aberrant proliferation, and blocked myelin regeneration after cuprizone-induced demyelination. Single-nucleus transcriptomics showed extensive transcriptional reprogramming in WWOX-deficient oligodendroglia during remyelination, with enrichment of WNT/TGFβ signaling and cell-cycle programs. Mechanistically, WWOX was shown to physically interact with SOX10 and stabilize SOX10 protein via its WW1 domain, linking WWOX to disrupted myelin gene network activity. This paper does not explicitly discuss endometriosis or adenomyosis; it was included in the corpus via a keyword match in the upstream search index.

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Abstract

Summary Remyelination is essential for neuronal function and plasticity, and its failure contributes to multiple sclerosis (MS) and other neurodegenerative disorders. Yet, the molecular programs governing oligodendrocyte precursor cell (OPC) differentiation and remyelination remain incompletely defined. Here, we identify the WW domain–containing oxidoreductase (WWOX) as a critical cell-autonomous regulator of oligodendrocyte differentiation and myelin repair. Reanalysis of single-nucleus RNA sequencing from MS lesions revealed WWOX as one of the most significantly dysregulated oligodendroglial genes. Conditional deletion of Wwox in oligodendroglia impaired OPC differentiation, favouring aberrant proliferation and blocking myelin regeneration after cuprizone-induced demyelination. Single-nucleus transcriptomics confirmed profound transcriptional reprogramming in WWOX-deficient oligodendroglia during remyelination, with enrichment of WNT and TGFβ signalling and cell cycle programs. Mechanistically, WWOX physically interacts with the master transcription factor SOX10 via its WW1 domain, stabilising SOX10 protein and sustaining its downstream myelin gene network. Loss of WWOX reduced SOX10 stability and activity, providing a direct mechanistic link to defective OPC differentiation. Together, our findings uncover WWOX as an essential orchestrator of remyelination and position the WWOX–SOX10 axis as a promising therapeutic target for enhancing myelin repair in MS and related demyelinating disorders.
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Summary Remyelination is essential for neuronal function and plasticity, and its failure contributes to multiple sclerosis (MS) and other neurodegenerative disorders. Yet, the molecular programs governing oligodendrocyte precursor cell (OPC) differentiation and remyelination remain incompletely defined. Here, we identify the WW domain–containing oxidoreductase (WWOX) as a critical cell-autonomous regulator of oligodendrocyte differentiation and myelin repair. Reanalysis of single-nucleus RNA sequencing from MS lesions revealed WWOX as one of the most significantly dysregulated oligodendroglial genes. Conditional deletion of Wwox in oligodendroglia impaired OPC differentiation, favouring aberrant proliferation and blocking myelin regeneration after cuprizone-induced demyelination. Single-nucleus transcriptomics confirmed profound transcriptional reprogramming in WWOX-deficient oligodendroglia during remyelination, with enrichment of WNT and TGFβ signalling and cell cycle programs. Mechanistically, WWOX physically interacts with the master transcription factor SOX10 via its WW1 domain, stabilising SOX10 protein and sustaining its downstream myelin gene network. Loss of WWOX reduced SOX10 stability and activity, providing a direct mechanistic link to defective OPC differentiation. Together, our findings uncover WWOX as an essential orchestrator of remyelination and position the WWOX–SOX10 axis as a promising therapeutic target for enhancing myelin repair in MS and related demyelinating disorders. Competing Interest Statement R.I.A. is a consultant for Mahzi Therapeutics. The other authors declare no competing interests.

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