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Updated: Jun 3, 2026

Skeletal Phenotype Analysis of a Conditional Stat3 Deletion Mouse Model
Published on: July 3, 2020
Ubiquitin C-terminal hydrolase-L3 regulates Smad1 ubiquitination and osteoblast differentiation
Ji Young Kim1, Jae-Mok Lee, Je-Yoel Cho
1Department of Biochemistry, School of Dentistry, Kyungpook National University, Daegu, South Korea.
Abstract:
Ubiquitin C-terminal hydrolase-L3 (Uch-L3), a deubiquitinating enzyme, is upregulated in bone morphogenetic protein 2-induced osteoblast differentiation. The mechanism and role of Uch-L3 in the process of osteoblast differentiation is unknown. We found that Uch-L3 physically interacts with Smad1 and dramatically decreases the amount of poly-ubiquitinated Smad1. Osteoblast differentiation was enhanced in the C2C12 cells stably transfected with Uch-L3. Otherwise, the siRNA knock-down of Uch-L3 resulted in the decrease of osteoblast differentiation. These results suggest that Uch-L3 enhances osteoblast differentiation through the stabilization of Smad1 signaling. Thus, Uch-L3 acts to fine-tune the process of Smad1 activation.
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