Malerba M, Bianchetti R
Dipartimento di Biotecnologie e Bioscienze, Università degli Studi di Milano-Bicocca, Piazza della Scienza 2, Milan, 20126, Italy.
Biochem Biophys Res Commun. 2001 Sep 7;286(5):984-90. doi: 10.1006/bbrc.2001.5506.
Several authors previously showed that the interaction between 14-3-3 proteins and plasma membrane H(+)-ATPase leads to an activated complex in which the enzyme is endowed with more favorable kinetic parameters and a more physiological pH optimum. In this paper we report immunological studies with antibodies covering a different specific region of the protein, including the N- and the C-terminal ends. The results showed that, beside a free and a complexed form, a third form of H(+)-ATPase in the cell must exist with low activity and no more activation due to the loss of a part of the C-terminal regulatory domain. A model in which 14-3-3 proteins activate H(+)-ATPase by protecting it from a specific proteolytic attack is presented and its generalization is discussed.
几位作者之前表明，14-3-3蛋白与质膜H(+) -ATP酶之间的相互作用会导致形成一种活化复合物，其中该酶具有更有利的动力学参数和更接近生理状态的最适pH值。在本文中，我们报道了用覆盖该蛋白不同特定区域（包括N端和C端）的抗体进行的免疫学研究。结果表明，除了游离形式和复合形式外，细胞中必然存在第三种形式的H(+) -ATP酶，其活性较低，且由于C端调节域部分缺失而不再具有激活作用。本文提出了一个模型，即14-3-3蛋白通过保护H(+) -ATP酶免受特定蛋白水解攻击来激活它，并讨论了该模型的普遍性。
