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Ubiquitin C-terminal hydrolase-L3 Regulates Smad1 Ubiquitination and Osteoblast Differentiation

Ubiquitin C-terminal hydrolase-L3 Regulates Smad1 Ubiquitination and Osteoblast Differentiation

Ji Young Kim, Jae-Mok Lee, Je-Yoel Cho

FEBS Lett. 2011 Apr 20;585(8):1121-6.

PMID: 21453705

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR4241402	Ubiquitin C-terminal Hydrolase-L3			Price

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