Isolation of 88F Actin Mutants of and Possible Alterations in the Mutant Actin Structures

An, HyeSuck; Mogami, Kaname

doi:10.1006/jmbi.1996.0417

Cited by 36 publications

(19 citation statements)

References 48 publications

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“…The effect is particularly pronounced in several antimorphic alleles in which DMLC2 is not detected at all. (11) These results are consistent with the proposal that DMLC2 interacts with actin, perhaps through its extended N terminus. (38) More importantly, however, these results indicate that the assembly of functional thin and thick myofilaments may not be as independent of each other as is often assumed.…”

Section: Proteomicssupporting

confidence: 91%

Genetics of the Drosophila flight muscle myofibril: a window into the biology of complex systems

Vigoreaux

2001

BioEssays

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This essay reviews the long tradition of experimental genetics of the Drosophila indirect flight muscles (IFM). It discusses how genetics can operate in tandem with multidisciplinary approaches to provide a description, in molecular terms, of the functional properties of the muscle myofibril. In particular, studies at the interface of genetics and proteomics address protein function at the cellular scale and offer an outstanding platform with which to elucidate how the myofibril works. Two generalizations can be enunciated from the studies reviewed. First, the study of mutant IFM proteomes provides insight into how proteins are functionally organized in the myofibril. Second, IFM mutants can give rise to structural and contractile defects that are unrelated, a reflection of the dual function that myofibrillar proteins play as fundamental components of the sarcomeric framework and biochemical "parts" of the contractile "engine".

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Section: Proteomicssupporting

confidence: 91%

Genetics of the Drosophila flight muscle myofibril: a window into the biology of complex systems

Vigoreaux

2001

BioEssays

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“…The hydrophobic plug mutation G268R, which incorporated into normal actin structures in NIH3T3 despite reduced co-polymerization capacity, is an example of one of these. When G268D was expressed homozygously in the indirect flight muscle of Drosophila melanogaster, it induced wavy fibers but the heterozygote was normal (An and Mogami, 1996). L267D in yeast actin resulted in a mild phenotype (a cold-sensitive polymerization defect) (Chen et al, 1993).…”

Section: Discussionmentioning

confidence: 99%

Myopathy mutations in α-skeletal-muscle actin cause a range of molecular defects

Costa

Rommelaere

Waterschoot

et al. 2004

Journal of Cell Science

120

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“…Hypercontraction is a phenomenon that leads to muscle defects like thinning and tearing, following uncontrolled actomyosin interactions of otherwise normally assembled sarcomeric structures (Nongthomba et al 2003). Mutations leading to hypercontraction have been localized in structural genes such as the upheld gene (up 101 ) (Fyrberg et al 1990;Nongthomba et al 2003), flightin (fln 0 ) (Reedy et al 2000), Actin88F (An and Mogami 1996;Nongthomba et al 2003), Myosin heavy chain (Mhc 6 , Mhc 13 , and Mhc 19 ) (Kronert et al 1995), wings up A (wupA hdp-2 ) (Beall and Fyrberg 1991;Nongthomba et al 2003), the protein phosphatase genes flapwing (flw 1 , flw 6 , and flw 7 ) (Raghavan et al 2000;Pronovost et al 2013), and calcineurin B2 (canB2 EP(2)0774 ) (Gajewski et al 2006). Mutations producing hypercontraction fall in a large repertoire of proteins, suggesting that there could be multiple grounds for reaching the phenotype.…”

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confidence: 99%

A cis-Regulatory Mutation in Troponin-I of Drosophila Reveals the Importance of Proper Stoichiometry of Structural Proteins During Muscle Assembly

et al. 2015

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Rapid and high wing-beat frequencies achieved during insect flight are powered by the indirect flight muscles, the largest group of muscles present in the thorax. Any anomaly during the assembly and/or structural impairment of the indirect flight muscles gives rise to a flightless phenotype. Multiple mutagenesis screens in Drosophila melanogaster for defective flight behavior have led to the isolation and characterization of mutations that have been instrumental in the identification of many proteins and residues that are important for muscle assembly, function, and disease. In this article, we present a molecular-genetic characterization of a flightless mutation, flightless-H (fliH), originally designated as heldup-a (hdp-a). We show that fliH is a cis-regulatory mutation of the wings up A (wupA) gene, which codes for the troponin-I protein, one of the troponin complex proteins, involved in regulation of muscle contraction. The mutation leads to reduced levels of troponin-I transcript and protein. In addition to this, there is also coordinated reduction in transcript and protein levels of other structural protein isoforms that are part of the troponin complex. The altered transcript and protein stoichiometry ultimately culminates in unregulated acto-myosin interactions and a hypercontraction muscle phenotype. Our results shed new insights into the importance of maintaining the stoichiometry of structural proteins during muscle assembly for proper function with implications for the identification of mutations and disease phenotypes in other species, including humans.

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Isolation of 88F Actin Mutants of and Possible Alterations in the Mutant Actin Structures

Cited by 36 publications

References 48 publications

Genetics of the Drosophila flight muscle myofibril: a window into the biology of complex systems

Genetics of the Drosophila flight muscle myofibril: a window into the biology of complex systems

Myopathy mutations in α-skeletal-muscle actin cause a range of molecular defects

A cis-Regulatory Mutation in Troponin-I of Drosophila Reveals the Importance of Proper Stoichiometry of Structural Proteins During Muscle Assembly

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