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    Please use this identifier to cite or link to this item: http://ir.nhri.org.tw/handle/3990099045/15362


    Title: The prolyl isomerase Pin1 stabilizes NeuroD during differentiation of mechanoreceptors
    Authors: Zhao, L;Fong, SH;Yang, Q;Jiang, YJ;Korzh, V;Liou, YC
    Contributors: Institute of Molecular and Genomic Medicine
    Abstract: The peptidyl prolyl cis-trans isomerase Pin1 plays vital roles in diverse cellular processes and pathological conditions. NeuroD is a differentiation and survival factor for a subset of neurons and pancreatic endocrine cells. Although multiple phosphorylation events are known to be crucial for NeuroD function, their mechanisms remain elusive. In this study, we demonstrate that zebrafish embryos deficient in Pin1 displayed phenotypes resembling those associated with NeuroD depletion, characterized by defects in formation of mechanosensory hair cells. Furthermore, zebrafish Pin1 interacts with NeuroD in a phosphorylation-dependent manner. In Pin1-deficient cell lines, NeuroD is rapidly degraded. However, the protein stability of NeuroD is restored upon overexpression of Pin1. These findings suggest that Pin1 functionally regulates NeuroD protein levels by post-phosphorylation cis-trans isomerization during neuronal specification.
    Date: 2023-09-18
    Relation: Frontiers in Cell and Developmental Biology. 2023 Sep 18;11:Article number 1225128.
    Link to: https://doi.org/10.3389/fcell.2023.1225128
    JIF/Ranking 2023: http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=NHRI&SrcApp=NHRI_IR&KeyISSN=2296-634X&DestApp=IC2JCR
    Cited Times(WOS): https://www.webofscience.com/wos/woscc/full-record/WOS:001074428100001
    Cited Times(Scopus): https://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85173916470
    Appears in Collections:[江運金] 期刊論文

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