Reconstitution of water channel function of aquaporins 1 and 2 by expression in yeast secretory vesicles Export

@article{citeulike:4070815, abstract = {Aquaporins 1 (AQP1) and 2 (AQP2) were expressed in the yeast secretory mutant sec6-4. The mutant accumulates post-Golgi, plasma membrane-targeted vesicles and may be used to produce large quantities of membrane proteins. AQP1 or AQP2 were inducibly expressed in yeast and were localized within isolated sec6-4 vesicles by immunoblot analysis. Secretory vesicles containing AQP1 and AQP2 exhibited high water permeabilities and low activation energies for water flow, indicating expression of functional AQP1 and AQP2. AQP1 solubilized from secretory vesicles was successfully reconstituted into proteoliposomes, demonstrating the ability to use the yeast system to express aquaporins for reconstitution studies. The AQP2-containing secretory vesicles showed no increased permeability toward formamide, urea, glycerol, or protons compared with control vesicles, demonstrating that AQP2 is highly selective for water over these other substances. We conclude that the expression of aquaporins in yeast sec6 vesicles is a valid system to further study mammalian water channel function.}, author = {Coury, Larry A. and Mathai, John C. and Prasad, Ramesh G. V. . and Brodsky, Jeffrey L. and Agre, Peter and Zeidel, Mark L.}, citeulike-article-id = {4070815}, citeulike-linkout-0 = {http://ajprenal.physiology.org/cgi/content/abstract/274/1/F34}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/9458821}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=9458821}, day = {1}, journal = {Am J Physiol Renal Physiol}, keywords = {qqp, transport, water}, month = {January}, number = {1}, pages = {F34--42}, posted-at = {2009-02-19 11:25:51}, priority = {2}, title = {Reconstitution of water channel function of aquaporins 1 and 2 by expression in yeast secretory vesicles}, url = {http://ajprenal.physiology.org/cgi/content/abstract/274/1/F34}, volume = {274}, year = {1998} }

TY - JOUR ID - citeulike:4070815 L3 - citeulike-article-id:4070815 N2 - Aquaporins 1 (AQP1) and 2 (AQP2) were expressed in the yeast secretory mutant sec6-4. The mutant accumulates post-Golgi, plasma membrane-targeted vesicles and may be used to produce large quantities of membrane proteins. AQP1 or AQP2 were inducibly expressed in yeast and were localized within isolated sec6-4 vesicles by immunoblot analysis. Secretory vesicles containing AQP1 and AQP2 exhibited high water permeabilities and low activation energies for water flow, indicating expression of functional AQP1 and AQP2. AQP1 solubilized from secretory vesicles was successfully reconstituted into proteoliposomes, demonstrating the ability to use the yeast system to express aquaporins for reconstitution studies. The AQP2-containing secretory vesicles showed no increased permeability toward formamide, urea, glycerol, or protons compared with control vesicles, demonstrating that AQP2 is highly selective for water over these other substances. We conclude that the expression of aquaporins in yeast sec6 vesicles is a valid system to further study mammalian water channel function. IS - 1 JF - Am J Physiol Renal Physiol EP - 42 TI - Reconstitution of water channel function of aquaporins 1 and 2 by expression in yeast secretory vesicles VL - 274 SP - F34 KW - qqp KW - transport KW - water AU - Coury, Larry AU - Mathai, John AU - Prasad, Ramesh AU - Brodsky, Jeffrey AU - Agre, Peter AU - Zeidel, Mark PY - 1998/01/01/ UR - http://ajprenal.physiology.org/cgi/content/abstract/274/1/F34 ER -