ArticleThe Journal of cell biology1994
The unconventional myosin, Myo2p, is a calmodulin target at sites of cell growth in Saccharomyces cerevisiae.
Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 108 citations in OpenAlex.
- Progress of Antimicrobial Mechanisms of Stilbenoids.Pharmaceutics · 2024Review
- Yeast Rgd3 is a phospho-regulated F-BAR-containing RhoGAP involved in the regulation of Rho3 distribution and cell morphology.Molecular biology of the cell · 2020Article
- Essential genetic interactors of SIR2 required for spatial sequestration and asymmetrical inheritance of protein aggregates.PLoS genetics · 2014Article
- Proteomic Evaluation of Cellular Responses of Saccharomyces cerevisiae to Formic Acid Stress.Mycobiology · 2010Article
- Antifungal activity of tamoxifen: in vitro and in vivo activities and mechanistic characterization.Antimicrobial agents and chemotherapy · 2009Article
- A molecular dynamics study and free energy analysis of complexes between the Mlc1p protein and two IQ motif peptides.Biophysical journal · 2006Article
- Cytokinesis depends on the motor domains of myosin-II in fission yeast but not in budding yeast.Molecular biology of the cell · 2005Article
- Structure of the light chain-binding domain of myosin V.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Calcium- and calcineurin-independent roles for calmodulin in Cryptococcus neoformans morphogenesis and high-temperature growth.Eukaryotic cell · 2005Article
- Binding of calmodulin to Nuf1p is required for karyogamy in Saccharomyces cerevisiae.Molecular genetics and genomics : MGG · 2003Article
- She4p/Dim1p interacts with the motor domain of unconventional myosins in the budding yeast, Saccharomyces cerevisiae.Molecular biology of the cell · 2003Article
- Two distinct myosin light chain structures are induced by specific variations within the bound IQ motifs-functional implications.The EMBO journal · 2003Article
- Remodeling of organelle-bound actin is required for yeast vacuole fusion.The Journal of cell biology · 2002Article
- Identification of two type V myosins in fission yeast, one of which functions in polarized cell growth and moves rapidly in the cell.Molecular biology of the cell · 2001Article
- The secretory pathway mediates localization of the cell polarity regulator Aip3p/Bud6p.Molecular biology of the cell · 2000Article
- The terminal tail region of a yeast myosin-V mediates its attachment to vacuole membranes and sites of polarized growth.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- The yeast centrin, cdc31p, and the interacting protein kinase, Kic1p, are required for cell integrity.The Journal of cell biology · 1998Article
- Identification of functional connections between calmodulin and the yeast actin cytoskeleton.Genetics · 1998Article
- Mlc1p is a light chain for the unconventional myosin Myo2p in Saccharomyces cerevisiae.The Journal of cell biology · 1998Article
- Spatial regulation of exocytosis: lessons from yeast.The Journal of cell biology · 1998Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Myo2p is an unconventional myosin required for polarized growth in Saccharomyces cerevisiae. Four lines of evidence suggest that (a) Myo2p is a target of calmodulin at sites of cell growth, and (b) the interaction between Myo2p and calmodulin is Ca2+ independent. First, as assessed by indirect immunofluorescence, the distributions of Myo2p and calmodulin are nearly indistinguishable throughout the cell cycle. Second, a genetic analysis indicates that mutations in CMD1 show allele-specific synthetic lethality with the myo2-66 conditional mutation. Mutations that inactivate the Ca(2+)-binding sites of calmodulin have little or no effect on strains carrying myo2-66, whereas an allele with a mutation outside the Ca(2+)-binding sites dramatically increases the severity of the phenotype conferred by myo2-66. Third, Myo2p coimmunoprecipitates with calmodulin in the presence of Ca2+ or EGTA. Finally, we used a modified gel overlay assay to demonstrate direct interaction between calmodulin and fusion proteins containing portions of Myo2p. Calmodulin binds specifically to the region of Myo2p containing six tandem repeats of a motif called an IQ site. Binding occurs in either Ca2+ or EGTA, and only two sites are required to observe binding.
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