Activation of H+-ATPase by glucose in Saccharomyces cerevisiae involves a membrane serine protease

MONESTEROLO, N.E.; PREVITALI, G.; SANTANDER, V.S.; AMAIDEN, M.R.; ARCE, C.A.; VALDEZ-TAUBAS, JAVIER; CASALE, C.H.

ELSEVIER SCIENCE BV

Lugar: Amsterdam; Año: 2013 vol. 1830 p. 3593 - 3593

ackground: Glucose induces H 24 +-ATPase activation in Saccharomyces cerevisiae. Our previous study showed Q3 that (i) S. cerevisiae plasma membrane H 25 +-ATPase forms a complex with acetylated tubulin (AcTub), resulting in inhibition of the enzyme activity; (ii) exogenous glucose addition results in the dissociation of the complex 26 and recovery of the enzyme activity. 27 Methods: We used classic biochemical and molecular biology tools in order to identify the key components in 28 the mechanism that leads to H 29 +-ATPase activation after glucose treatment. Results: We demonstrate that glucose-induced dissociation of the complex is due to pH-dependent activation of 30 a protease that hydrolyzes membrane tubulin. Biochemical analysis identified a serine protease with a kDa of 31 35?40 and an isoelectric point between 8 and 9. Analysis of several knockout yeast strains led to the detection 32 of Lpx1p as the serine protease responsible of tubulin proteolysis. When lpx1Δ