Prolyl isomerase Pin1 regulates the osteogenic activity of Osterix. (15th January 2015)

• Record Type: Journal Article
• Authors: Lee, Sung Ho; Jeong, Hyung Min; Han, Younho; Cheong, Heesun; Kang, Bok Yun; Lee, Kwang Youl
• Is Part Of: Molecular and cellular endocrinology. Volume 400(2015)
• Page Start: 32
• Page End: 40
• Publication Date: 2015-01-15
• Subjects: Pin1 -- Osterix -- Osteoblast differentiation; Endocrinology -- Periodicals; Molecular biology -- Periodicals; Cytology -- Periodicals; Endocrinology -- Periodicals; Hormones -- Periodicals; Endocrinologie -- Périodiques; Cytology; Endocrinology; Molecular biology; Periodicals; 573.4
• DOI: 10.1016/j.mce.2014.11.017
• Languages: English
• ISSNs: 0303-7207

Abstract

Highlights: Pin1 interacts with Osterix. Pin1 increases the protein stability of Osterix. Pin1 enhances transcriptional activity of Osterix. Abstract: Osterix is an essential transcription factor for osteoblast differentiation and bone formation. The mechanism of regulation of Osterix by post-translational modification remains unknown. Peptidyl-prolyl isomerase 1 (Pin1) catalyzes the isomerization of pSer/Thr-Pro bonds and induces a conformational change in its substrates, subsequently regulating diverse cellular processes. In this study, we demonstrated that Pin1 interacts with Osterix and influences its protein stability and transcriptional activity. This regulation is likely due to the suppression of poly-ubiquitination-mediated proteasomal degradation of Osterix. Collectively, our data demonstrate that Pin1 is a novel regulator of Osterix and may play an essential role in the regulation of osteogenic differentiation.