INVESTIGADORES
MONESTEROLO Noelia Edith
congresos y reuniones científicas
Título:
INTERACTION OF TUBULIN WITH H+-ATPase OF PLASMA MEMBRANE IN SACCHAROMYCES CEREVISIAE. INFLUENCE OF GLUCOSE UPTAKE.
Autor/es:
ALEXIS N. CAMPETELLI; GABRIELA PREVITALI; NOELIA MONESTEROLO; CARLOS A. ARCE; HÉCTOR S. BARRA; CESAR CASALE
Lugar:
Iguazù,Misiones, Argentina
Reunión:
Congreso; SAIB 2004; 2004
Institución organizadora:
Sociedad Argentina de Investigacion Bioquimica y Biologia Molecular
Resumen:
It was previously
reported that Na+,K+-ATPase in membranes of
brain and
cultured astrocytes interacts with tubulin and that this
interaction
inhibits the enzyme activity. Dissociation of the tubulin/
Na+,K+-ATPase
complex leads to activation of the enzyme and to
a lesser amount
of hydrophobic tubulin. In the present study we
investigated the
eventual interaction of tubulin with H+-ATPase
in yeast
membranes. We found that the acetylated tubulin is present
in plasma
membrane of yeast and interacts with H+-ATPase. We
demonstrate that
this interaction inhibits the enzyme activity. In
effect, when
isolated membranes were treated with tubulin purified
from brain, we
found inhibition of H+-ATPase in a degree that
was higher when
the tubulin preparation contained higher
proportion of the
acetylated isoform. It is known that H+-ATPase
is activated by
the addition of D-glucose into the culture medium.
As expected,
after treatment of the cells with glucose, we found
an inverse
correlation between the activation of H+-ATPase and
the amount of
acetylated tubulin associated with the enzyme.
Addition of 1 mM
2-deoxy-D-Glucose (inhibitor of D-Glucose
transport) after
D-glucose treatment reversed the effects of DGlucose.
These results
indicate that the H+-ATPase activity of S.
cerevisiae is
modulated by the association/dissociation of
(acetylated tubulin-H+-ATPase) complex..