Lu Te-Jung, Huang Chi-Ying F, Yuan Chiun-Jye, Lee Yuan-Chii, Leu Tzeng-Horng, Chang Wen-Chang, Lu Te-Ling, Jeng Wen-Yih, Lai Ming-Derg
Department of Biochemistry and Molecular Biology, College of Medicine, National Cheng Kung University, Tainan.
J Inorg Biochem. 2005 Jun;99(6):1306-13. doi: 10.1016/j.jinorgbio.2005.03.003.
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), Zn(2+), and Co(2+)) 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. Mn(2+), Co(2+), and Mg(2+)-dependent autophosphorylation of MST3 is mainly on threonine residue while Zn(2+)-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 Zn(2+) as the metal ion cofactor of a recombinant serine/threonine kinase.
我们研究了Ste20丝氨酸/苏氨酸激酶家族中MST3（哺乳动物Ste20样激酶3）对金属离子辅因子的偏好。四种金属离子（Mg(+2)、Mn(+2)、Zn(2+)和Co(2+)）在生理浓度范围内激活内源性、外源性和杆状病毒表达的重组MST3。相比之下，Fe(+2)和Ca(+2)不能作为MST3的辅因子。MST3的Mn(2+)、Co(2+)和Mg(2+)依赖性自磷酸化主要发生在苏氨酸残基上，而Zn(2+)刺激的MST3自磷酸化则发生在丝氨酸和苏氨酸残基上。MST3上不同的自磷酸化模式表明，MST3可能根据所使用的金属离子辅因子的类型发挥各种类型的激酶反应。据我们所知，这是首次报道显示Zn(2+)作为重组丝氨酸/苏氨酸激酶的金属离子辅因子。
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