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    Proteolytic processing of secretory pathway kinase Fam20C by site-1 protease promotes biomineralization, PNAS, 5 Aug 2021

    發布時間:2021年08月05日

    PNAS, 5 August, 2021, DOI:https://doi.org/10.1073/pnas.2100133118

    Proteolytic processing of secretory pathway kinase Fam20C by site-1 protease promotes biomineralization

    Xinxin Chen, Jianchao Zhang, Pulan Liu, Yangyang Wei, Xi’e Wang, Junyu Xiao, Chih-chen Wang, and Lei Wang 

    Abstract

    Family with sequence similarity 20C (Fam20C), the major protein kinase in the secretory pathway, generates the vast majority of the secreted phosphoproteome. However, the regulatory mechanisms of Fam20C transport, secretion, and function remain largely unexplored. Here, we show that Fam20C exists as a type II transmembrane protein within the secretory compartments, with its N-terminal signal peptide-like region serving as a membrane anchor for Golgi retention. The secretion and kinase activity of Fam20C are governed by site-1 protease (S1P), a key regulator of cholesterol homeostasis. We find that only mature Fam20C processed by S1P functions in osteoblast differentiation and mineralization. Together, our findings reveal a unique mechanism for Fam20C secretion and activation via proteolytic regulation, providing a molecular link between biomineralization and lipid metabolism.

    文章鏈接:https://www.pnas.org/content/118/32/e2100133118

    相關報道:http://www.kevinscanvas.com/kyjz/zxdt/202108/t20210806_6153254.html

     

     

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