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MARCH2 suppresses odontoblast differentiation by polyubiquitinating PTPRD.
Hao Feng1,2,3, Jiaxin Niu1,2,3, Zhi Chen1
1State Key Laboratory of Oral & Maxillofacial Reconstruction and Regeneration, Key Laboratory of Oral Biomedicine Ministry of Education, Hubei Key Laboratory of Stomatology, School & Hospital of Stomatology, Wuhan University, Wuhan, China.
International Journal of Oral Science
|January 9, 2026
Summary
Membrane-associated RING finger protein 2 (March2) inhibits dentin formation by promoting the degradation of protein tyrosine phosphatase receptor delta (PTPRD). This discovery reveals a new regulatory mechanism for odontoblast differentiation.
Area of Science:
- Biochemistry
- Cell Biology
- Developmental Biology
Background:
- Dentin, a key dental tissue, is formed by odontoblasts, but the regulation of their differentiation is poorly understood.
- Membrane-associated RING finger protein 2 (March2) shows increased expression during odontoblast differentiation.
Purpose of the Study:
- To investigate the role of March2 in regulating odontoblast differentiation.
- To elucidate the molecular mechanism by which March2 influences dentin formation.
Main Methods:
- Screening of March family members expression.
- Knockdown and overexpression experiments in mouse dental papilla cells (mDPCs).
- Analysis of March2-deficient and odontoblast-specific March2 knockdown mice.
- Co-immunoprecipitation and ubiquitination assays to study protein interactions and degradation pathways.
Main Results:
- March2 expression is highest among March family members and increases during odontoblast differentiation.
- March2 inhibits mDPC differentiation and dentin deposition.
- March2 interacts with PTPRD, promoting its K27-linked polyubiquitination and lysosomal degradation.
- Knockdown of PTPRD impairs odontoblast differentiation, and its double knockdown with March2 rescues the differentiation defect.
Conclusions:
- March2 acts as an E3 ubiquitin ligase that inhibits odontoblast differentiation by degrading PTPRD.
- This study uncovers a novel regulatory pathway involving E3 ubiquitin ligase-mediated protein degradation in dentinogenesis.
- March2 represents a potential therapeutic target for enhancing dentin repair and regeneration.
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