Arce Carlos A, Casale Cesar H, Barra Héctor S
Centro de Investigaciones en Química Biológica de Córdoba, Departamento de Química Biológica, Universidad Nacional de Córdoba,Argentina.
FEBS J. 2008 Oct;275(19):4664-74. doi: 10.1111/j.1742-4658.2008.06615.x. Epub 2008 Aug 27.
The ATP-hydrolysing enzymes (Na(+),K(+))-, H(+)- and Ca(2+)-ATPase are integral membrane proteins that play important roles in the exchange of ions and nutrients between the exterior and interior of cells, and are involved in signal transduction pathways. Activity of these ATPases is regulated by several specific effectors. Here, we review the regulation of these P-type ATPases by a common effector, acetylated tubulin, which interacts with them and inhibits their enzyme activity. The presence of an acetyl group on Lys40 of alpha-tubulin is a requirement for the interaction. Stimulation of enzyme activity by different effectors involves the dissociation of tubulin/ATPase complexes. In cultured cells, acetylated tubulin associated with ATPase appears to be a constituent of microtubules. Stabilization of microtubules by taxol blocks association/dissociation of the complex. Membrane ATPases may function as anchorage sites for microtubules.
ATP水解酶（钠钾ATP酶）、氢ATP酶和钙ATP酶是整合膜蛋白，在细胞内外离子和营养物质交换中起重要作用，并参与信号转导途径。这些ATP酶的活性受多种特定效应物调节。在此，我们综述了一种常见效应物——乙酰化微管蛋白对这些P型ATP酶的调节作用，乙酰化微管蛋白与它们相互作用并抑制其酶活性。α微管蛋白赖氨酸40位存在乙酰基团是相互作用的必要条件。不同效应物对酶活性的刺激涉及微管蛋白/ATP酶复合物的解离。在培养细胞中，与ATP酶相关的乙酰化微管蛋白似乎是微管的一个组成部分。紫杉醇对微管的稳定作用阻止了复合物的结合/解离。膜ATP酶可能作为微管的锚定位点。
