Submembraneous microtubule cytoskeleton: Regulation of ATPases by interaction with acetylated tubulin

ARCE, C.A.; CASALE, C.H.; BARRA, H. S

WILEY-BLACKWELL PUBLISHING, INC

Año: 2008 vol. 275 p. 4664 - 4664

p class="MsoNormal" style="MARGIN: 0cm 0cm 0pt; LINE-HEIGHT: 150%; tab-stops: 28.8pt">Abstract The ATP-hydrolysing enzymes (Na+,K+)-, H+- and Ca2+- 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