國家衛生研究院 NHRI:Item 3990099045/2247
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    Please use this identifier to cite or link to this item: http://ir.nhri.org.tw/handle/3990099045/2247


    Title: Zinc ion acts as a cofactor for serine/threonine kinase MST3 and has a distinct role in autophosphorylation of MST3
    Authors: Lu, TJ;Huang, CYF;Yuan, CJ;Lee, YC;Leu, TH;Chang, WC;Lu, TL;Jeng, WY;Lai, MD
    Contributors: Division of Molecular and Genomic Medicine
    Abstract: We examined the metal ion cofactor preference for MST3 (mammalian Ste20-like kinase 3) of the Ste20 serine/threonine kinase family. Four metal ions (Mg+2, Mn+2, Zn2+, and Co2+) activate endogenous, exogenous, and baculovirus-expressed recombinant MST3 within the physiological concentration range. In contrast, Fe+2 and Ca+2 do not function as MST3 cofactors. Mn2+, Co2+, and Mg2+-dependent autophosphorylation of MST3 is mainly on threonine residue while Zn2+-stimulated MST3 autophosphorylation is on both serine and threonine residues. The distinct autophosphorylation pattern on MST3 suggests that MST3 may exert various types of kinase reactions depending on the type of metal ion cofactor used. To our knowledge, this is the first report showing Zn2+ as the metal ion cofactor of a recombinant serine/threonine kinase. (C) 2005 Elsevier Inc. All rights reserved.
    Keywords: Biochemistry & Molecular Biology;Chemistry, Inorganic & Nuclear
    Date: 2005-06
    Relation: Journal of Inorganic Biochemistry. 2005 Jun;99(6):1306-1313.
    Link to: http://dx.doi.org/10.1016/j.jinorgbio.2005.03.003
    JIF/Ranking 2023: http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=NHRI&SrcApp=NHRI_IR&KeyISSN=0162-0134&DestApp=IC2JCR
    Cited Times(WOS): https://www.webofscience.com/wos/woscc/full-record/WOS:000229702200005
    Cited Times(Scopus): http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=19444365622
    Appears in Collections:[Chi-Ying F. Huang(1998-2005)] Periodical Articles

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