Difference between revisions of "YLL043W"
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| − | '''Description of YLL043W:''' Plasma membrane channel, member of major intrinsic protein (MIP) family; involved in efflux of glycerol and in uptake of acetic acid and the trivalent metalloids arsenite and antimonite; phosphorylated by Hog1p MAPK under acetate stress | + | '''Description of YLL043W:''' Plasma membrane channel, member of major intrinsic protein (MIP) family; involved in efflux of glycerol and in uptake of acetic acid and the trivalent metalloids arsenite and antimonite; phosphorylated by Hog1p MAPK under acetate stress<ref name='S000046364'>Luyten K, et al. (1995) Fps1, a yeast member of the MIP family of channel proteins, is a facilitator for glycerol uptake and efflux and is inactive under osmotic stress. EMBO J 14(7):1360-71 {{SGDpaper|S000046364}} PMID 7729414</ref><ref name='S000123333'>Mollapour M and Piper PW (2007) Hog1 mitogen-activated protein kinase phosphorylation targets the yeast fps1 aquaglyceroporin for endocytosis, thereby rendering cells resistant to acetic Acid. Mol Cell Biol 27(18):6446-56 {{SGDpaper|S000123333}} PMID 17620418</ref><ref name='S000044207'>Tamas MJ, et al. (1999) Fps1p controls the accumulation and release of the compatible solute glycerol in yeast osmoregulation. Mol Microbiol 31(4):1087-104 {{SGDpaper|S000044207}} PMID 10096077</ref><ref name='S000060866'>Wysocki R, et al. (2001) The glycerol channel Fps1p mediates the uptake of arsenite and antimonite in Saccharomyces cerevisiae. Mol Microbiol 40(6):1391-401 |
| − | {{SGDpaper| | + | {{SGDpaper|S000060866}} PMID 11442837</ref> |
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Revision as of 13:05, 25 February 2010
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| Systematic name | YLL043W |
| Gene name | FPS1 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr XII:49937..51946 |
| Primary SGDID | S000003966 |
Description of YLL043W: Plasma membrane channel, member of major intrinsic protein (MIP) family; involved in efflux of glycerol and in uptake of acetic acid and the trivalent metalloids arsenite and antimonite; phosphorylated by Hog1p MAPK under acetate stress[1][2][3][4]
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Contents
Community Commentary
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Protein Details
Protein Function/Process
Disruption of the FPS1 gene for the aquaglyceroporin Fps1p reduced uptake of 73As(III) into cells, conferring resistance to arsenite. The arsenate-resistant phenotype could be functionally complemented by expression of AQP9, a mammalian homologue [5] [6]
The main role of Fps1 is export of glycerol for osmoregulation. Fps1 transport function is gated to ensure glycerol accummulation and glycerol release depending on osmotic conditions. The mechanism of gating is not fully understood but requires certain conserved domains of Fps1 and, directly or indirectly, the Hog1 MAPK.
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References
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- ↑ Luyten K, et al. (1995) Fps1, a yeast member of the MIP family of channel proteins, is a facilitator for glycerol uptake and efflux and is inactive under osmotic stress. EMBO J 14(7):1360-71 SGD PMID 7729414
- ↑ Mollapour M and Piper PW (2007) Hog1 mitogen-activated protein kinase phosphorylation targets the yeast fps1 aquaglyceroporin for endocytosis, thereby rendering cells resistant to acetic Acid. Mol Cell Biol 27(18):6446-56 SGD PMID 17620418
- ↑ Tamas MJ, et al. (1999) Fps1p controls the accumulation and release of the compatible solute glycerol in yeast osmoregulation. Mol Microbiol 31(4):1087-104 SGD PMID 10096077
- ↑ Wysocki R, et al. (2001) The glycerol channel Fps1p mediates the uptake of arsenite and antimonite in Saccharomyces cerevisiae. Mol Microbiol 40(6):1391-401 SGD PMID 11442837
- ↑ Liu Z, et al. (2002) Arsenite transport by mammalian aquaglyceroporins AQP7 and AQP9. Proc Natl Acad Sci U S A 99(9):6053-8 SGD PMID 11972053
- ↑ submitted by Barry Rosen on 2003-07-31
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References
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