YLL043W - Revision history

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S Hohmann: /* Community Commentary */

2007-06-23T05:06:07Z

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2007-05-04T15:08:59Z

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@@ Line 4: / Line 4: @@
 {|{{Prettytable}} align = 'right' width = '200px'
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003966 YLL043W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003966 YLL043W]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''FPS1 ''

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr XII:49937..51946
+|nowrap| Chr XII:49938..51947
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000003966

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''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='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='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='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|S000060866}} PMID 11442837</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
+'''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|S000123333}} PMID 17620418</ref>
+  {{SGDpaper|S000060866}} PMID 11442837</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''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='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='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|S000060866}} PMID 11442837</ref><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='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
+'''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='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='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='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|S000060866}} PMID 11442837</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|S000044207}} PMID 10096077</ref>
+  {{SGDpaper|S000123333}} PMID 17620418</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YLL043W:''' Plasma membrane glycerol channel, member of the major intrinsic protein (MIP) family of channel proteins; involved in efflux of glycerol and in uptake of the trivalent metalloids arsenite and antimonite<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|S000060866}} PMID 11442837</ref><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='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
+'''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='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='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|S000060866}} PMID 11442837</ref><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='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>
 <br>

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-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 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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 <protect>
 ==References==
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← Older revision		Revision as of 20:02, 21 February 2007
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		+	<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->
		+	<!--
		+	Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
		+	<ref>Boer VM, et al. (2003) The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur.
		+	J Biol Chem 278(5):3265-74</ref>
		+	-->

	<protect>		<protect>