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首页> 外文期刊>Molecular and Cellular Biology >The interaction of small domains between the subunits of phosphatidylinositol 3-kinase determines enzyme activity.
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The interaction of small domains between the subunits of phosphatidylinositol 3-kinase determines enzyme activity.

机译：磷脂酰肌醇3-激酶亚基之间的小结构域的相互作用决定了酶的活性。

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Previous studies have suggested that the two subunits of phosphatidylinositol (PI) 3-kinase, p85 and p110, function as localizing and catalytic subunits, respectively. Using recombinant p85 and p110 molecules, we have reconstituted the specific interaction between the two subunits of mouse PI 3-kinase in cells and in vitro. We have previously shown that the region between the two Src homology 2 (SH2) domains of p85 is able to form a functional complex with the 110-kDa subunit in vivo. In this report, we identify the corresponding domain in p110 which directs the binding to p85. We demonstrate that the interactive domains in p85 and p110 are less than 103 and 124 amino acids, respectively, in size. We also show that the association of p85 and p110 mediated by these domains is critical for PI 3-kinase activity. Surprisingly, a complex between a 102-amino-acid segment of p85 and the full-length p110 molecule is catalytically active, whereas p110 alone has no activity. In addition to the catalytic domain in the carboxy-terminal region, 123 amino acids at the amino terminus of p110 were required for catalytic activity and were sufficient for the interaction with p85. These results indicate that the 85-kDa subunit, previously thought to have only a linking role in localizing the p110 catalytic subunit, is an important component of the catalytic complex.
机译：先前的研究表明，磷脂酰肌醇（PI）3-激酶的两个亚基p85和p110分别起定位和催化亚基的作用。使用重组p85和p110分子，我们已经重建了小鼠PI 3-激酶的两个亚基在细胞和体外的特异性相互作用。先前我们已经表明，p85的两个Src同源2（SH2）域之间的区域能够在体内与110-kDa亚基形成功能复合物。在此报告中，我们确定了p110中的相应域，该域将绑定引导至p85。我们证明p85和p110中的相互作用域分别小于103和124个氨基酸。我们还显示由这些域介导的p85和p110的关联对于PI 3-激酶活性至关重要。出人意料的是，p85的102个氨基酸段与全长p110分子之间的复合物具有催化活性，而单独的p110没有活性。除羧基末端区域的催化结构域外，p110氨基末端的123个氨基酸对于催化活性也是必需的，并且足以与p85相互作用。这些结果表明，以前认为在定位p110催化亚基中仅具有连接作用的85 kDa亚基是催化复合物的重要组成部分。

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