Other names published for CMD1: CaM, YBR109C
CMD1 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Cell Cycle Phase Involved
- Cellular Location
- Function/Process
- Genetic Interactions
- Mutants/Phenotypes
- Regulation of
- Regulatory Role
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
CMD1 - Genetic Interactions (20)
| Reference | Other Genes Addressed |
|---|---|
| Connolly S and Kingsbury T (2012) Regulatory subunit myristoylation antagonizes calcineurin phosphatase activation in yeast. J Biol Chem 287(47):39361-8 | |
| Kus B, et al. (2005) A high throughput screen to identify substrates for the ubiquitin ligase Rsp5. J Biol Chem 280(33):29470-8 | |
| Okano H, et al. (2004) A novel mechanism of intragenic complementation between Phe to Ala calmodulin mutations. J Biochem 135(3):289-95 | |
| Okano H and Ohya Y (2003) Binding of calmodulin to Nuf1p is required for karyogamy in Saccharomyces cerevisiae. Mol Genet Genomics 269(5):649-57 | |
| Schaerer-Brodbeck C and Riezman H (2003) Genetic and biochemical interactions between the Arp2/3 complex, Cmd1p, casein kinase II, and Tub4p in yeast. FEMS Yeast Res 4(1):37-49 | |
| 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 | |
| Schaerer-Brodbeck C and Riezman H (2000) Functional interactions between the p35 subunit of the Arp2/3 complex and calmodulin in yeast. Mol Biol Cell 11(4):1113-27 | |
| Schaerer-Brodbeck C and Riezman H (2000) Saccharomyces cerevisiae Arc35p works through two genetically separable calmodulin functions to regulate the actin and tubulin cytoskeletons. J Cell Sci 113 ( Pt 3):521-32 | |
| Geli MI, et al. (1998) Distinct functions of calmodulin are required for the uptake step of receptor-mediated endocytosis in yeast: the type I myosin Myo5p is one of the calmodulin targets. EMBO J 17(3):635-47 | |
| Sekiya-Kawasaki M, et al. (1998) Identification of functional connections between calmodulin and the yeast actin cytoskeleton. Genetics 150(1):43-58 | |
| Zhu G and Davis TN (1998) The fork head transcription factor Hcm1p participates in the regulation of SPC110, which encodes the calmodulin-binding protein in the yeast spindle pole body. Biochim Biophys Acta 1448(2):236-44 | |
| Danielsson A, et al. (1996) A genetic analysis of the role of calcineurin and calmodulin in Ca++-dependent improvement of NaCl tolerance of Saccharomyces cerevisiae. Curr Genet 30(6):476-84 | |
| Moser MJ, et al. (1996) Ca2+-calmodulin promotes survival of pheromone-induced growth arrest by activation of calcineurin and Ca2+-calmodulin-dependent protein kinase. Mol Cell Biol 16(9):4824-31 | |
| Stirling DA, et al. (1996) Mutations which block the binding of calmodulin to Spc110p cause multiple mitotic defects. J Cell Sci 109 ( Pt 6)():1297-310 | |
| Sundberg HA, et al. (1996) Role of calmodulin and Spc110p interaction in the proper assembly of spindle pole body compenents. J Cell Biol 133(1):111-24 | |
| Brockerhoff SE, et al. (1994) The unconventional myosin, Myo2p, is a calmodulin target at sites of cell growth in Saccharomyces cerevisiae. J Cell Biol 124(3):315-23 | |
| Ohya Y and Botstein D (1994) Structure-based systematic isolation of conditional-lethal mutations in the single yeast calmodulin gene. Genetics 138(4):1041-54 | |
| Stirling DA, et al. (1994) Interaction with calmodulin is required for the function of Spc110p, an essential component of the yeast spindle pole body. EMBO J 13(18):4329-42 | |
| Geiser JR, et al. (1993) The essential mitotic target of calmodulin is the 110-kilodalton component of the spindle pole body in Saccharomyces cerevisiae. Mol Cell Biol 13(12):7913-24 | |
| Zhu G, et al. (1993) A dosage-dependent suppressor of a temperature-sensitive calmodulin mutant encodes a protein related to the fork head family of DNA-binding proteins. Mol Cell Biol 13(3):1779-87 |



