Difference between revisions of "YCR009C"

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{|{{Prettytable}} align = 'right' width = '200px'
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YCR009C YCR009C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000602 YCR009C]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''RVS161 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''RVS161 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|nowrap| Chr III:131540..130743
 
|nowrap| Chr III:131540..130743
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000000602
 
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'''Description of {{PAGENAME}}:''' Amphiphysin-like lipid raft protein; subunit of a complex (Rvs161p-Rvs167p) that regulates polarization of the actin cytoskeleton, endocytosis, cell polarity, cell fusion and viability following starvation or osmotic stress<ref name='S000074856'>Lombardi R and Riezman H (2001) Rvs161p and Rvs167p, the two yeast amphiphysin homologs, function together in vivo. J Biol Chem 276(8):6016-22 {{SGDpaper|S000074856}} PMID 11096097</ref><ref name='S000054139'>Munn AL, et al. (1995) end5, end6, and end7: mutations that cause actin delocalization and block the internalization step of endocytosis in Saccharomyces cerevisiae. Mol Biol Cell 6(12):1721-42 {{SGDpaper|S000054139}} PMID 8590801</ref><ref name='S000045636'>Brizzio V, et al. (1998) Rvs161p interacts with Fus2p to promote cell fusion in Saccharomyces cerevisiae. J Cell Biol 141(3):567-84 {{SGDpaper|S000045636}} PMID 9566960</ref><ref name='S000045533'>Sivadon P, et al. (1995) Actin cytoskeleton and budding pattern are altered in the yeast rvs161 mutant: the Rvs161 protein shares common domains with the brain protein amphiphysin. Mol Gen Genet 246(4):485-95 {{SGDpaper|S000045533}} PMID 7891662</ref><ref name='S000042817'>Crouzet M, et al. (1991) Yeast mutant affected for viability upon nutrient starvation: characterization and cloning of the RVS161 gene. Yeast 7(7):727-43 {{SGDpaper|S000042817}} PMID 1776363</ref><ref name='S000039395'>Navarro P, et al. (1997) Protein-protein interaction between the RVS161 and RVS167 gene products of Saccharomyces cerevisiae. Biochim Biophys Acta 1343(2):187-92
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'''Description of YCR009C:''' Amphiphysin-like lipid raft protein; subunit of a complex (Rvs161p-Rvs167p) that regulates polarization of the actin cytoskeleton, endocytosis, cell polarity, cell fusion and viability following starvation or osmotic stress<ref name='S000074856'>Lombardi R and Riezman H (2001) Rvs161p and Rvs167p, the two yeast amphiphysin homologs, function together in vivo. J Biol Chem 276(8):6016-22 {{SGDpaper|S000074856}} PMID 11096097</ref><ref name='S000054139'>Munn AL, et al. (1995) end5, end6, and end7: mutations that cause actin delocalization and block the internalization step of endocytosis in Saccharomyces cerevisiae. Mol Biol Cell 6(12):1721-42 {{SGDpaper|S000054139}} PMID 8590801</ref><ref name='S000045636'>Brizzio V, et al. (1998) Rvs161p interacts with Fus2p to promote cell fusion in Saccharomyces cerevisiae. J Cell Biol 141(3):567-84 {{SGDpaper|S000045636}} PMID 9566960</ref><ref name='S000045533'>Sivadon P, et al. (1995) Actin cytoskeleton and budding pattern are altered in the yeast rvs161 mutant: the Rvs161 protein shares common domains with the brain protein amphiphysin. Mol Gen Genet 246(4):485-95 {{SGDpaper|S000045533}} PMID 7891662</ref><ref name='S000042817'>Crouzet M, et al. (1991) Yeast mutant affected for viability upon nutrient starvation: characterization and cloning of the RVS161 gene. Yeast 7(7):727-43 {{SGDpaper|S000042817}} PMID 1776363</ref><ref name='S000039395'>Navarro P, et al. (1997) Protein-protein interaction between the RVS161 and RVS167 gene products of Saccharomyces cerevisiae. Biochim Biophys Acta 1343(2):187-92
 
  {{SGDpaper|S000039395}} PMID 9434108</ref>
 
  {{SGDpaper|S000039395}} PMID 9434108</ref>
 
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J Biol Chem 278(5):3265-74</ref>
 
J Biol Chem 278(5):3265-74</ref>
 
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Revision as of 07:45, 27 February 2007

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Systematic name YCR009C
Gene name RVS161
Aliases END6, FUS7, SPE161
Feature type ORF, Verified
Coordinates Chr III:131540..130743
Primary SGDID S000000602


Description of YCR009C: Amphiphysin-like lipid raft protein; subunit of a complex (Rvs161p-Rvs167p) that regulates polarization of the actin cytoskeleton, endocytosis, cell polarity, cell fusion and viability following starvation or osmotic stress[1][2][3][4][5][6]




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References

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  1. Lombardi R and Riezman H (2001) Rvs161p and Rvs167p, the two yeast amphiphysin homologs, function together in vivo. J Biol Chem 276(8):6016-22 SGD PMID 11096097
  2. Munn AL, et al. (1995) end5, end6, and end7: mutations that cause actin delocalization and block the internalization step of endocytosis in Saccharomyces cerevisiae. Mol Biol Cell 6(12):1721-42 SGD PMID 8590801
  3. Brizzio V, et al. (1998) Rvs161p interacts with Fus2p to promote cell fusion in Saccharomyces cerevisiae. J Cell Biol 141(3):567-84 SGD PMID 9566960
  4. Sivadon P, et al. (1995) Actin cytoskeleton and budding pattern are altered in the yeast rvs161 mutant: the Rvs161 protein shares common domains with the brain protein amphiphysin. Mol Gen Genet 246(4):485-95 SGD PMID 7891662
  5. Crouzet M, et al. (1991) Yeast mutant affected for viability upon nutrient starvation: characterization and cloning of the RVS161 gene. Yeast 7(7):727-43 SGD PMID 1776363
  6. Navarro P, et al. (1997) Protein-protein interaction between the RVS161 and RVS167 gene products of Saccharomyces cerevisiae. Biochim Biophys Acta 1343(2):187-92 SGD PMID 9434108

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