REGULATION OF ATPases BY INTERACTION WITH ACETYLATED TUBULIN

CAMPETELLI ALEXIS; SANTANDER VERONICA; CASALE CESAR; MONESTEROLO NOELIA; PREVITALI GABRIELA; CARLOS ARCE; BARRA HECTOR

Villa Giardino. Córdoba

Congreso; XVI Jornadas Científicas. Sociedad de Biología de Córdoba; 2007

Sociedad de Biología de Córdoba

(Na+,K+)-, H+- and Ca2+- ATPases are integral membrane proteins that play important roles in the exchange of ions and nutrients between exterior and interior of the cell. Involvement of these ATP-hydrolysing enzymes in signal transduction pathways has increased the interest for their study. The activity of these ATPases can be regulated by several specific effectors. This word summarizes the information regarding the regulation of the mentioned ATPases by a common effector, acetylated tubulin. This tubulin isotype interacts with these ATPases, and inhibits their enzymatic activities. The presence of an acetyl group on lysine 40 of á-tubulin is a requirement for the interaction. The stimulation of the ATPases activity by the specific effectors involves the dissociation of the tubulin/ATPase complexes.  In cultured cells, acetylated tubulin that is associated with ATPases is apparently constituent of microtubules. Stabilization of microtubules by taxol is an impediment for association/dissociation of the complexes. Membrane ATPases could function as anchorage sites for microtubules.