SGD-Wiki - User contributions [en]

YBR109C

2008-07-27T03:02:10Z

Tdavis: /* Community Commentary */

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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?dbid=S000000313 YBR109C]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''CMD1 ''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases''' ||''CaM''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type''' || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr II:458356..457913
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000000313
|}
 
'''Description of YBR109C:''' Calmodulin; Ca++ binding protein that regulates Ca++ independent processes (mitosis, bud growth, actin organization, endocytosis, etc.) and Ca++ dependent processes (stress-activated pathways), targets include Nuf1p, Myo2p and calcineurin<ref name='S000080958'>Starai VJ, et al. (2005) Ion regulation of homotypic vacuole fusion in Saccharomyces cerevisiae. J Biol Chem 280(17):16754-62 {{SGDpaper|S000080958}} PMID 15737991</ref><ref name='S000071160'>Desrivieres S, et al. (2002) Calmodulin controls organization of the actin cytoskeleton via regulation of phosphatidylinositol (4,5)-bisphosphate synthesis in Saccharomyces cerevisiae. Biochem J 366(Pt 3):945-51 {{SGDpaper|S000071160}} PMID 12079494</ref><ref name='S000066251'>Cyert MS (2001) Genetic analysis of calmodulin and its targets in Saccharomyces cerevisiae. Annu Rev Genet 35:647-72 {{SGDpaper|S000066251}} PMID 11700296</ref><ref name='S000062321'>Peters C and Mayer A (1998) Ca2+/calmodulin signals the completion of docking and triggers a late step of vacuole fusion. Nature 396(6711):575-80 {{SGDpaper|S000062321}} PMID 9859992</ref><ref name='S000062307'>Starovasnik MA, et al. (1993) Similarities and differences between yeast and vertebrate calmodulin: an examination of the calcium-binding and structural properties of calmodulin from the yeast Saccharomyces cerevisiae. Biochemistry 32(13):3261-70 {{SGDpaper|S000062307}} PMID 8461293</ref><ref name='S000047941'>Ohya Y and Botstein D (1994) Diverse essential functions revealed by complementing yeast calmodulin mutants. Science 263(5149):963-6 {{SGDpaper|S000047941}} PMID 8310294</ref><ref name='S000046694'>Davis TN, et al. (1986) Isolation of the yeast calmodulin gene: calmodulin is an essential protein. Cell 47(3):423-31 {{SGDpaper|S000046694}} PMID 3533275</ref><ref name='S000041618'>Kubler E, et al. (1994) Calcium-independent calmodulin requirement for endocytosis in yeast. EMBO J 13(23):5539-46
{{SGDpaper|S000041618}} PMID 7988551</ref>
 
 
 
 
 
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==Community Commentary==
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Summary of Davis lab calmodulin alleles:
 cmd1-1: temperature-sensitive defect in mitosis with very minor defect in bud growth.
<ref> Davis, T. N. (1992). A temperature-sensitive calmodulin mutant loses viability during mitosis. J. Cell Biol., 118:607-617.</ref>
 cmd1-3: temperature-sensitive defect in mitosis and complete defect in all Ca2+-dependent functions (unpublished and <ref>Geiser, J. R., D. van Tuinen, S. E. Brockerhoff, M. M. Neff, T. N. Davis. (1991). Can calmodulin function without binding calcium? Cell, 65, 949-959.</ref>)
 cmd1-6: no defect in mitosis, complete defect in all Ca2+-dependent functions (unpublished and <ref>Geiser, J. R., D. van Tuinen, S. E. Brockerhoff, M. M. Neff, T. N. Davis. (1991). Can calmodulin function without binding calcium? Cell, 65, 949-959.</ref>)
 cmd1-8: temperature-sensitive defect in bud growth (mild and only apparent at 38C) (unpublished)




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==References==

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YBR109C

2008-07-27T02:59:41Z

Tdavis: /* Community Commentary */

{{PageTop}}
<protect>
{|{{Prettytable}} align = 'right' width = '200px'
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000313 YBR109C]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''CMD1 ''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases''' ||''CaM''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type''' || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr II:458356..457913
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000000313
|}
 
'''Description of YBR109C:''' Calmodulin; Ca++ binding protein that regulates Ca++ independent processes (mitosis, bud growth, actin organization, endocytosis, etc.) and Ca++ dependent processes (stress-activated pathways), targets include Nuf1p, Myo2p and calcineurin<ref name='S000080958'>Starai VJ, et al. (2005) Ion regulation of homotypic vacuole fusion in Saccharomyces cerevisiae. J Biol Chem 280(17):16754-62 {{SGDpaper|S000080958}} PMID 15737991</ref><ref name='S000071160'>Desrivieres S, et al. (2002) Calmodulin controls organization of the actin cytoskeleton via regulation of phosphatidylinositol (4,5)-bisphosphate synthesis in Saccharomyces cerevisiae. Biochem J 366(Pt 3):945-51 {{SGDpaper|S000071160}} PMID 12079494</ref><ref name='S000066251'>Cyert MS (2001) Genetic analysis of calmodulin and its targets in Saccharomyces cerevisiae. Annu Rev Genet 35:647-72 {{SGDpaper|S000066251}} PMID 11700296</ref><ref name='S000062321'>Peters C and Mayer A (1998) Ca2+/calmodulin signals the completion of docking and triggers a late step of vacuole fusion. Nature 396(6711):575-80 {{SGDpaper|S000062321}} PMID 9859992</ref><ref name='S000062307'>Starovasnik MA, et al. (1993) Similarities and differences between yeast and vertebrate calmodulin: an examination of the calcium-binding and structural properties of calmodulin from the yeast Saccharomyces cerevisiae. Biochemistry 32(13):3261-70 {{SGDpaper|S000062307}} PMID 8461293</ref><ref name='S000047941'>Ohya Y and Botstein D (1994) Diverse essential functions revealed by complementing yeast calmodulin mutants. Science 263(5149):963-6 {{SGDpaper|S000047941}} PMID 8310294</ref><ref name='S000046694'>Davis TN, et al. (1986) Isolation of the yeast calmodulin gene: calmodulin is an essential protein. Cell 47(3):423-31 {{SGDpaper|S000046694}} PMID 3533275</ref><ref name='S000041618'>Kubler E, et al. (1994) Calcium-independent calmodulin requirement for endocytosis in yeast. EMBO J 13(23):5539-46
{{SGDpaper|S000041618}} PMID 7988551</ref>
 
 
 
 
 
</protect>
__TOC__
==Community Commentary==
{{CommentaryHelp}}
Summary of Davis lab calmodulin alleles:
 cmd1-1: temperature-sensitive defect in mitosis with very minor defect in bud growth.
<ref> Davis, T. N. (1992). A temperature-sensitive calmodulin mutant loses viability during mitosis. J. Cell Biol., 118:607-617.</ref>
 cmd1-3: temperature-sensitive defect in mitosis and complete defect in all Ca2+-dependent functions (unpublished and <ref>Geiser, J. R., D. van Tuinen, S. E. Brockerhoff, M. M. Neff, T. N. Davis. (1991). Can calmodulin function without binding calcium? Cell, 65, 949-959.</ref>)
 cmd1-6: no defect in mitosis, defective in all Ca2+-dependent functions (unpublished and <ref>Geiser, J. R., D. van Tuinen, S. E. Brockerhoff, M. M. Neff, T. N. Davis. (1991). Can calmodulin function without binding calcium? Cell, 65, 949-959.</ref>)
 cmd1-8: temperature-sensitive defect in bud growth (mild and only apparent at 38C) (unpublished)




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==References==

{{RefHelp}}
</protect>