Difference between revisions of "YBR109C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YBR109C YBR109C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000313 YBR109C]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''CMD1 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''CMD1 ''
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases'''          ||'' ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases'''          ||''CaM''
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type'''          || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type'''          || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
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|nowrap| Chr II:458356..457913
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|nowrap| Chr II:458362..457919
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000000313
 
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'''Description of {{PAGENAME}}:''' 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
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'''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='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='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='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='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><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='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='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='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
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  {{SGDpaper|S000041618}} PMID 7988551</ref>
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  {{SGDpaper|S000062307}} PMID 8461293</ref>
 
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==Community Commentary==
 
==Community Commentary==
 
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Summary of Davis lab calmodulin alleles:
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<br>cmd1-1:  temperature-sensitive defect in mitosis with very minor defect in bud growth.
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<ref> Davis, T. N. (1992).  A temperature-sensitive calmodulin mutant loses viability during mitosis.  J. Cell Biol., 118:607-617.</ref>
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<br> cmd1-3:  temperature-sensitive defect in mitosis and complete defect in all Ca<sup>2+</sup>-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>)
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<br>cmd1-6:  no defect in mitosis, complete defect in all Ca<sup>2+</sup>-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>)
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<br>cmd1-8:  temperature-sensitive defect in bud growth (mild and only apparent at 38C) (unpublished)
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Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
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<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.
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J Biol Chem 278(5):3265-74</ref>
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==References==
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Latest revision as of 07:45, 23 January 2012

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Systematic name YBR109C
Gene name CMD1
Aliases CaM
Feature type ORF, Verified
Coordinates Chr II:458362..457919
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[1][2][3][4][5][6][7][8]




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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. [9]
cmd1-3: temperature-sensitive defect in mitosis and complete defect in all Ca2+-dependent functions (unpublished and [10])
cmd1-6: no defect in mitosis, complete defect in all Ca2+-dependent functions (unpublished and [11])
cmd1-8: temperature-sensitive defect in bud growth (mild and only apparent at 38C) (unpublished)




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References

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  1. ↑ Cyert MS (2001) Genetic analysis of calmodulin and its targets in Saccharomyces cerevisiae. Annu Rev Genet 35:647-72 SGD PMID 11700296
  2. ↑ Davis TN, et al. (1986) Isolation of the yeast calmodulin gene: calmodulin is an essential protein. Cell 47(3):423-31 SGD PMID 3533275
  3. ↑ 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 SGD PMID 12079494
  4. ↑ Kubler E, et al. (1994) Calcium-independent calmodulin requirement for endocytosis in yeast. EMBO J 13(23):5539-46 SGD PMID 7988551
  5. ↑ Ohya Y and Botstein D (1994) Diverse essential functions revealed by complementing yeast calmodulin mutants. Science 263(5149):963-6 SGD PMID 8310294
  6. ↑ 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 SGD PMID 9859992
  7. ↑ Starai VJ, et al. (2005) Ion regulation of homotypic vacuole fusion in Saccharomyces cerevisiae. J Biol Chem 280(17):16754-62 SGD PMID 15737991
  8. ↑ 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 SGD PMID 8461293
  9. ↑ Davis, T. N. (1992). A temperature-sensitive calmodulin mutant loses viability during mitosis. J. Cell Biol., 118:607-617.
  10. ↑ 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.
  11. ↑ 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.

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References

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