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OALib Journal期刊
ISSN: 2333-9721
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过量表达的出芽酵母蛋白激酶ypk1磷酸化调控
DOI: 10.3724/SP.J.1145.2013.00241, PP. 241-248
Keywords: 出芽酵母,ypk1,pdk1位点,pdk2位点,磷酸化,胁迫应答,时序衰老
Abstract:
出芽酵母（saccharomycescerevisiae）中的ypk1与人体蛋白激酶sgk（humanserum-andglucocorticoid-induciblekinase）同源.ypk1的504位苏氨酸残基是其激活环内的磷酸化位点，也称之为pdk1位点，而662位苏氨酸残基是位于其疏水区的pdk2位点，这两个位点的磷酸化对其激酶活性非常重要.对ypk1过量表达后其pdk1和pdk2位点的磷酸化调控研究结果显示，ypk1过量表达后其pdk1和pdk2位点磷酸化水平在对数生长期呈现递增趋势，至平台期趋于稳定并在7d的时序衰老过程中始终维持较高的磷酸化水平.在野生型细胞中分别过量表达ypk1t504a和ypk1t662a两个突变体会导致细胞对渗透压胁迫敏感性增加.而短暂渗透压胁迫处理会导致过量表达的ypk1的pdk1和pdk2位点部分去磷酸化.研究结果表明过量表达的ypk1的pdk1和pdk2位点磷酸化在出芽酵母时序衰老及胁迫应答过程中发挥着重要作用.图5参16
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