The Saccharomyces cerevisiae strain Sigma 1278b possesses two putative aqua
porins, Aqy1-1p and Aqy2-1p. Previous work demonstrated that Aqy1-1p functi
ons as a water channel in Xenopus oocyte. However, no function could be att
ributed to Aqy2-1p in this system. Specific antibodies were used to follow
the expression of Aqy1-1p and Aqy2-1p in the yeast. Aqy1-1p was never detec
ted whatever the growth phase and culture conditions tested. In contrast, A
qy2-1p was detected only during the exponential growth phase in rich medium
containing glucose. Aqy2-1p expression was repressed by hyper-osmotic cult
ure conditions. Both immunocytochemistry and biochemical subcellular fracti
onation demonstrated that Aqy2-1p is located on the endoplasmic reticulum (
ER) as well as on the plasma membrane. In microsomal vesicles enriched in E
R, a water channel activity due to Aqy2-1p was detected by stopped-flow ana
lysis. Our results show that the expression of aquaporins is tightly contro
lled. The physiological relevance of aquaporin-mediated water transport in
yeast is discussed.