SIGNAL TRANSDUCTION IN SACCHAROMYCES-CEREVISIAE REQUIRES TYROSINE AND THREONINE PHOSPHORYLATION OF FUS3 AND KSS1
SIGNAL TRANSDUCTION IN SACCHAROMYCES-CEREVISIAE REQUIRES TYROSINE AND THREONINE PHOSPHORYLATION OF FUS3 AND KSS1
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DOI：
10.1101/gad.6.7.1280
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发表时间：
1992-07-01
影响因子：
10.5
通讯作者：
AMMERER, G
中科院分区：
文献类型：
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作者：
GARTNER, A;NASMYTH, K;AMMERER, G
FUS3和KSS1激酶是酵母信息素依赖信号转导途径的组成部分。我们发现FUS3和KSS1在信息素处理后迅速磷酸化。与哺乳动物的MAP激酶类似，这种修饰发生在FUS3的两个氨基酸上，苏氨酸-180和酪氨酸-182。在任何一个位置引入突变都会导致体内功能的完全丧失。破坏激酶催化活性的氨基酸取代不能阻止突变产物的磷酸化，这一结果排除了自催化激活途径。FUS3的修饰依赖于STE11和STE7基因编码的激酶。此外，在没有信息素刺激的情况下，一个过度活跃的STE11等位基因会导致FUS3磷酸化增加。因此，STE7或STE11都可能是负责FUS3磷酸化的激酶。
The FUS3 and KSS1 kinases are components of the pheromone-dependent signal transduction pathway in yeast. We show that FUS3 and KSS1 become rapidly phosphorylated after pheromone treatment. Similar to mammalian MAP kinases, this modification occurs at two amino acids of FUS3, threonine-180 and tyrosine-182. A mutation introduced at either position results in complete loss of function in vivo. Amino acid substitutions that destroy catalytic activity of the kinase do not prevent phosphorylation of the mutant products, a result that excludes an autocatalytic activation pathway. The modification of FUS3 is dependent on kinases encoded by the STE11 and STE7 genes. Furthermore, a hyperactive allele of STE11 causes increased phosphorylation of FUS3 in the absence of pheromone stimulation. Thus, either STE7 or STE11 could be the kinase responsible for the phosphorylation of FUS3.