Yeast · 2011 · 23 citations · 26 references
Life SciencesBiochemistryMolecular BiologyMembrane BiochemistryMembrane BiophysicsMembrane ScienceChannel StructureIon ChannelsMembrane PermeabilityMembrane ProteinsMembrane TransportOsmosisAquaporin PhysiologyAquaporin RegulationAquaporin TransportAquaporin-mediated TransportAquaporin-mediated Water TransportAquaporinsMip ClassWater Transport In Cells
The Saccharomyces cerevisiae Fps1 glycerol channel is a member of the major intrinsic protein (MIP) family of plasma membrane channel proteins that functions in osmoregulatory pathways to transport glycerol passively out of the cell. The MIP family is subdivided into members that are selectively permeable to water (aquaporins) and those permeated by glycerol (aquaglyceroporins or glycerol facilitators). Although aquaporins function as homo-tetramers with each monomer possessing its own channel, previous studies have suggested that aquaglyceroporins may function as monomers. Here we provide both genetic and biochemical evidence that Fps1 functions as a homotetramer to regulate glycerol transport in yeast.
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Structural determinants of water permeation through aquaporin-1
Kazuyoshi Murata, Kaoru Mitsuoka, Teruhisa Hirai et al. · Nature · 2000 · 1.8K citations
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Haixin Sui, Bong-Gyoon Han, John K. Lee et al. · Nature · 2001 · 1.1K citations · Full text
Structure of a Glycerol-Conducting Channel and the Basis for Its Selectivity
Andrew M. Libson, Larry J. W. Miercke, Cindy Weitzman et al. · Science · 2000 · 999 citations