The mechanism of activation of PMCA by calmodulin or etanol involves dissociation of tubulin/PMCA complex.

MONESTEROLO, N; PREVITALI, G; CARLOS ANGEL ARCE; BARRA, H.S.; CASALE, C.H.

WILEY-BLACKWELL PUBLISHING, INC

Año: 2008 vol. 275 p. 3567 - 3567

p class="MsoNormal" style="MARGIN: 0cm -71pt 0pt 0cm; TEXT-INDENT: 35.3pt; TEXT-ALIGN: justify">We showed recently that acetylated tubulin interacts with plasma membrane Na+,K+-ATPase and inhibits its enzyme activity in several types of cells. H+-ATPase of S. cerevisiae is similarly inhibited by interaction with acetylated tubulin. Activities of both these ATPases are restored upon dissociation of the acetylated tubulin/ATPase complex. We now report that in plasma membrane vesicles isolated from brain synaptosomes, another P-type ATPase, plasma membrane Ca2+-ATPase (PMCA), undergoes enzyme activity regulation by its association/dissociation with acetylated tubulin. Presence of acetylated tubulin/PMCA complex in membrane vesicles was demonstrated by analyzing the behaviour of acetylated tubulin in detergent partition, and by immunoprec