Spontaneous avoidance behavior in Drosophila null for calmodulin expression.

Heiman, Robert G.; Atkinson, Richard C.; Andruss, Bernard F.; Bolduc, Clare; Kovalick, Gae E.; Beckingham, Kathy

doi:10.1073/pnas.93.6.2420

Cited by 55 publications

(43 citation statements)

References 39 publications

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“…In Drosophila, CaM is encoded by a single gene, cam [170,171], and null mutations in cam are lethal [172]. Mosaic flies missing cam from the eye display developmental defects.…”

Section: Ca 2+ -Dependent Termination Of the Photoresponsementioning

confidence: 99%

Phototransduction and retinal degeneration in Drosophila

Wang

Montell

2007

Pflugers Arch - Eur J Physiol

261

303

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Drosophila visual transduction is the fastest known G-protein-coupled signaling cascade and has therefore served as a genetically tractable animal model for characterizing rapid responses to sensory stimulation. Mutations in over 30 genes have been identified, which affect activation, adaptation, or termination of the photoresponse. Based on analyses of these genes, a model for phototransduction has emerged, which involves phosphoinoside signaling and culminates with opening of the TRP and TRPL cation channels. Many of the proteins that function in phototransduction are coupled to the PDZ containing scaffold protein INAD and form a supramolecular signaling complex, the signalplex. Arrestin, TRPL, and Gα q undergo dynamic light-dependent trafficking, and these movements function in long-term adaptation. Other proteins play important roles either in the formation or maturation of rhodopsin, or in regeneration of phosphatidylinositol 4,5-bisphosphate (PIP 2 ), which is required for the photoresponse. Mutation of nearly any gene that functions in the photoresponse results in retinal degeneration. The underlying bases of photoreceptor cell death are diverse and involve mechanisms such as excessive endocytosis of rhodopsin due to stable rhodopsin/arrestin complexes and abnormally low or high levels of Ca 2+ . Drosophila visual transduction appears to have particular relevance to the cascade in the intrinsically photosensitive retinal ganglion cells in mammals, as the photoresponse in these latter cells appears to operate through a remarkably similar mechanism.

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“…In Drosophila, CaM is encoded by a single gene, cam [170,171], and null mutations in cam are lethal [172]. Mosaic flies missing cam from the eye display developmental defects.…”

Section: Ca 2+ -Dependent Termination Of the Photoresponsementioning

confidence: 99%

Phototransduction and retinal degeneration in Drosophila

Wang

Montell

2007

Pflugers Arch - Eur J Physiol

261

303

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“…Calmodulin is encoded by essential genes in Drosophila melanogaster, Aspergillus nidulans, Saccharomyces cerevisiae, and Schizosaccharomyces pombe (13,23,30,42). Given that the cam1-ts mutant cells express less than 2% of the wild-type level of calmodulin mRNA, we sought to test if CAM1 is an essential gene and if this reduced level is sufficient to maintain cell viability or alternatively whether the CAM1 gene is dispensable for viability in C. neoformans at 25°C but required at 37°C.…”

Section: An Insertional Mutagenesis Screen For High-temperature Growtmentioning

confidence: 99%

Calcium- and Calcineurin-Independent Roles for Calmodulin in Cryptococcus neoformans Morphogenesis and High-Temperature Growth

Kraus¹,

Nichols²,

Heitman

2005

Eukaryot Cell

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The function of calcium as a signaling molecule is conserved in eukaryotes from fungi to humans. Previous studies have identified the calcium-activated phosphatase calcineurin as a critical factor in governing growth of the human pathogenic fungus Cryptococcus neoformans at mammalian body temperature. Here, we employed insertional mutagenesis to identify new genes required for growth at 37°C. One insertion mutant, cam1-ts, that displayed a growth defect at 37°C and hypersensitivity to the calcineurin inhibitor FK506 at 25°C was isolated. Both phenotypes were linked to the dominant marker in genetic crosses, and molecular analysis revealed that the insertion occurred in the 3 untranslated region of the gene encoding the calcineurin activator calmodulin (CAM1) and impairs growth at 37°C by significantly reducing calmodulin mRNA abundance. The CAM1 gene was demonstrated to be essential using genetic analysis of a CAM1/cam1⌬ diploid strain. In the absence of calcineurin function, the cam1-ts mutant displayed a severe morphological defect with impaired bud formation. Expression of a calmodulin-independent calcineurin mutant did not suppress the growth defect of the cam1-ts mutant at 37°C, indicating that calmodulin promotes growth at high temperature via calcineurin-dependent and -independent pathways. In addition, a Ca 2؉ -binding-defective allele of CAM1 complemented the 37°C growth defect, FK506 hypersensitivity, and morphogenesis defect of the cam1-ts mutant. Our findings reveal that calmodulin performs Ca 2؉ -and calcineurin-independent and -dependent roles in controlling C. neoformans morphogenesis and high-temperature growth.

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“…Studies in yeast (9) and Drosophila (10) revealed that CaM is an indispensable gene. Although there is less sequence identity between yeast and animal CaMs (60% identity) than among most animal CaMs, human CaM could functionally complement yeast CaM (11).…”

mentioning

confidence: 99%

Interaction of a Kinesin-like Protein with Calmodulin Isoforms from Arabidopsis

Reddy

Safadi

Zielinski

et al. 1999

Journal of Biological Chemistry

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In Arabidopsis and other plants there are multiple calmodulin isoforms. However, the role of these isoforms in regulating the activity of target proteins is obscure. Here, we analyzed the interaction between a kinesin-like calmodulin-binding motor protein (Reddy, A. S. N., Safadi, F., Narasimhulu, S. B., Golovkin, M., and Hu, X. (1996) J. Biol. Chem. 271, 7052-7060) and three calmodulin isoforms (calmodulin-2, -4, and -6) from Arabidopsis using different approaches. Gel mobility and fluorescence shift assays revealed that the motor binds to all calmodulin isoforms in a calcium-dependent manner. Furthermore, all calmodulin isoforms were able to activate bovine calcium/calmodulin-dependent phosphodiesterase. However, the concentration of calmodulin-2 required for half-maximal activation of phosphodiesterase is 2-and 6-fold lower compared with calmodulin-4 and -6, respectively. The dissociation constants of the motor to calmodulin-2, -4, and -6 are 12.8, 27.0, and 27.8 nM, respectively, indicating that calmodulin-2 has 2-fold higher affinity for the motor than calmodulin-4 and -6. Similar results were obtained using another assay that involves the binding of 35 S-labeled calmodulin isoforms to the motor. The binding saturation curves of the motor with calmodulin isoforms have confirmed that calmodulin-2 has 2-fold higher affinity to the motor. However, the affinity of calmodulin-4 and -6 isoforms for the motor was about the same. Based on these studies, we conclude that all calmodulin isoforms bind to the motor protein but with different affinities.

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Spontaneous avoidance behavior in Drosophila null for calmodulin expression.

Cited by 55 publications

References 39 publications

Phototransduction and retinal degeneration in Drosophila

Phototransduction and retinal degeneration in Drosophila

Calcium- and Calcineurin-Independent Roles for Calmodulin in Cryptococcus neoformans Morphogenesis and High-Temperature Growth

Interaction of a Kinesin-like Protein with Calmodulin Isoforms from Arabidopsis

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