YBR109C
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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cmd1-3: temperature-sensitive defect in mitosis and complete defect in all Ca2+-dependent functions (unpublished and [10])
cmd1-6: no defect in mitosis, complete defect in all Ca2+-dependent functions (unpublished and [11])
cmd1-8: temperature-sensitive defect in bud growth (mild and only apparent at 38C) (unpublished)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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- ↑ Cyert MS (2001) Genetic analysis of calmodulin and its targets in Saccharomyces cerevisiae. Annu Rev Genet 35:647-72 SGD PMID 11700296
- ↑ Davis TN, et al. (1986) Isolation of the yeast calmodulin gene: calmodulin is an essential protein. Cell 47(3):423-31 SGD PMID 3533275
- ↑ 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
- ↑ Kubler E, et al. (1994) Calcium-independent calmodulin requirement for endocytosis in yeast. EMBO J 13(23):5539-46 SGD PMID 7988551
- ↑ Ohya Y and Botstein D (1994) Diverse essential functions revealed by complementing yeast calmodulin mutants. Science 263(5149):963-6 SGD PMID 8310294
- ↑ 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
- ↑ Starai VJ, et al. (2005) Ion regulation of homotypic vacuole fusion in Saccharomyces cerevisiae. J Biol Chem 280(17):16754-62 SGD PMID 15737991
- ↑ 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
- ↑ Davis, T. N. (1992). A temperature-sensitive calmodulin mutant loses viability during mitosis. J. Cell Biol., 118:607-617.
- ↑ 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.
- ↑ 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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