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Journal articles on the topic 'Drosophila IFM'

Author: Grafiati

Published: 6 September 2023

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1

Loya, Amy K., Sarah K. Van Houten, Bernadette M. Glasheen, and Douglas M. Swank. "Shortening deactivation: quantifying a critical component of cyclical muscle contraction." American Journal of Physiology-Cell Physiology 322, no. 4 (2022): C653—C665. http://dx.doi.org/10.1152/ajpcell.00281.2021.

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A muscle undergoing cyclical contractions requires fast and efficient muscle activation and relaxation to generate high power with relatively low energetic cost. To enhance activation and increase force levels during shortening, some muscle types have evolved stretch activation (SA), a delayed increased in force following rapid muscle lengthening. SA’s complementary phenomenon is shortening deactivation (SD), a delayed decrease in force following muscle shortening. SD increases muscle relaxation, which decreases resistance to subsequent muscle lengthening. Although it might be just as importan

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2

Kreuz, A. J., A. Simcox, and D. Maughan. "Alterations in flight muscle ultrastructure and function in Drosophila tropomyosin mutants." Journal of Cell Biology 135, no. 3 (1996): 673–87. http://dx.doi.org/10.1083/jcb.135.3.673.

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Drosophila indirect flight muscle (IFM) contains two different types of tropomyosin: a standard 284-amino acid muscle tropomyosin, Ifm-TmI, encoded by the TmI gene, and two &gt; 400 amino acid tropomyosins, TnH-33 and TnH-34, encoded by TmII. The two IFM-specific TnH isoforms are unique tropomyosins with a COOH-terminal extension of approximately 200 residues which is hydrophobic and rich in prolines. Previous analysis of a hypomorphic TmI mutant, Ifm(3)3, demonstrated that Ifm-TmI is necessary for proper myofibrillar assembly, but no null TmI mutant or TmII mutant which affects the TnH is

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3

Gu, Wenzhi, Qiufang Li, Meng Ding, et al. "Regular Exercise Rescues Heart Function Defects and Shortens the Lifespan of Drosophila Caused by dMnM Downregulation." International Journal of Environmental Research and Public Health 19, no. 24 (2022): 16554. http://dx.doi.org/10.3390/ijerph192416554.

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Although studies have shown that myomesin 2 (MYOM2) mutations can lead to hypertrophic cardiomyopathy (HCM), a common cardiovascular disease that has a serious impact on human life, the effect of MYOM2 on cardiac function and lifespan in humans is unknown. In this study, dMnM (MYOM2 homologs) knockdown in cardiomyocytes resulted in diastolic cardiac defects (diastolic dysfunction and arrhythmias) and increased cardiac oxidative stress. Furthermore, the knockdown of dMnM in indirect flight muscle (IFM) reduced climbing ability and shortened lifespan. However, regular exercise significantly amel

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4

Glasheen, Bernadette M., Catherine C. Eldred, Leah C. Sullivan, et al. "Stretch activation properties of Drosophila and Lethocerus indirect flight muscle suggest similar calcium-dependent mechanisms." American Journal of Physiology-Cell Physiology 313, no. 6 (2017): C621—C631. http://dx.doi.org/10.1152/ajpcell.00110.2017.

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Muscle stretch activation (SA) is critical for optimal cardiac and insect indirect flight muscle (IFM) power generation. The SA mechanism has been investigated for decades with many theories proposed, but none proven. One reason for the slow progress could be that multiple SA mechanisms may have evolved in multiple species or muscle types. Laboratories studying IFM SA in the same or different species have reported differing SA functional properties which would, if true, suggest divergent mechanisms. However, these conflicting results might be due to different experimental methodologies. Thus,

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5

Kulke, Michael, Ciprian Neagoe, Bernhard Kolmerer, et al. "Kettin, a major source of myofibrillar stiffness in Drosophila indirect flight muscle." Journal of Cell Biology 154, no. 5 (2001): 1045–58. http://dx.doi.org/10.1083/jcb.200104016.

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Kettin is a high molecular mass protein of insect muscle that in the sarcomeres binds to actin and α-actinin. To investigate kettin's functional role, we combined immunolabeling experiments with mechanical and biochemical studies on indirect flight muscle (IFM) myofibrils of Drosophila melanogaster. Micrographs of stretched IFM sarcomeres labeled with kettin antibodies revealed staining of the Z-disc periphery. After extraction of the kettin-associated actin, the A-band edges were also stained. In contrast, the staining pattern of projectin, another IFM–I-band protein, was not altered by actin

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6

Zhao, Cuiping, and Douglas M. Swank. "The Drosophila indirect flight muscle myosin heavy chain isoform is insufficient to transform the jump muscle into a highly stretch-activated muscle type." American Journal of Physiology-Cell Physiology 312, no. 2 (2017): C111—C118. http://dx.doi.org/10.1152/ajpcell.00284.2016.

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Stretch activation (SA) is a delayed increase in force that enables high power and efficiency from a cyclically contracting muscle. SA exists in various degrees in almost all muscle types. In Drosophila, the indirect flight muscle (IFM) displays exceptionally high SA force production ( FSA), whereas the jump muscle produces only minimal FSA. We previously found that expressing an embryonic (EMB) myosin heavy chain (MHC) isoform in the jump muscle transforms it into a moderately SA muscle type and enables positive cyclical power generation. To investigate whether variation in MHC isoforms is su

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QIU, Feng, Anne LAKEY, Bogos AGIANIAN, et al. "Troponin C in different insect muscle types: identification of two isoforms in Lethocerus, Drosophila and Anopheles that are specific to asynchronous flight muscle in the adult insect." Biochemical Journal 371, no. 3 (2003): 811–21. http://dx.doi.org/10.1042/bj20021814.

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The indirect flight muscles (IFMs) of Lethocerus (giant water bug) and Drosophila (fruitfly) are asynchronous: oscillatory contractions are produced by periodic stretches in the presence of a Ca2+ concentration that does not fully activate the muscle. The troponin complex on thin filaments regulates contraction in striated muscle. The complex in IFM has subunits that are specific to this muscle type, and stretch activation may act through troponin. Lethocerus and Drosophila have an unusual isoform of the Ca2+-binding subunit of troponin, troponin C (TnC), with a single Ca2+-binding site near t

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8

Brault, V., M. C. Reedy, U. Sauder, R. A. Kammerer, U. Aebi, and C. Schoenenberger. "Substitution of flight muscle-specific actin by human (beta)-cytoplasmic actin in the indirect flight muscle of Drosophila." Journal of Cell Science 112, no. 21 (1999): 3627–39. http://dx.doi.org/10.1242/jcs.112.21.3627.

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The human (beta)-cytoplasmic actin differs by only 15 amino acids from Act88F actin which is the only actin expressed in the indirect flight muscle (IFM) of Drosophila melanogaster. To test the structural and functional significance of this difference, we ectopically expressed (beta)-cytoplasmic actin in the IFM of Drosophila that lack endogenous Act88F. When expression of the heterologous actin was regulated by approximately 1.5 kb of the 5′ promoter region of the Act88F gene, little (beta)-cytoplasmic actin accumulated in the IFM of the flightless transformants. Including Act88F-specific 5′

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9

Babu, Sajesh, and Nallur B. Ramachandra. "Screen for new mutations on the 2nd chromosome involved in indirect flight muscle development in Drosophila melanogaster." Genome 50, no. 4 (2007): 343–50. http://dx.doi.org/10.1139/g07-012.

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An extensive ethylmethanesulfonate mutagenesis of Drosophila melanogaster was undertaken to isolate the stronger alleles of 3 indirect flight-muscle mutations. We isolated 17 strong mutant lines, with nearly complete penetrance and expressivity, using direct screening under polarized light, from more than 1700 mutagenized chromosomes. On complementation, we found 11 of these 17 mutant lines to be alleles of 3 indirect flight-muscle mutations (Ifm(2)RU1, 3 noncomplementing lines; ifm(2)RU2, 6 alleles; ifm(2)RU3, 2 alleles) of the previously isolated 8 complementation groups (Ifm(2)RU1to ifm(2)R

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10

Reedy, Mary C., Belinda Bullard, and Jim O. Vigoreaux. "Flightin Is Essential for Thick Filament Assembly and Sarcomere Stability in Drosophila Flight Muscles." Journal of Cell Biology 151, no. 7 (2000): 1483–500. http://dx.doi.org/10.1083/jcb.151.7.1483.

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Flightin is a multiply phosphorylated, 20-kD myofibrillar protein found in Drosophila indirect flight muscles (IFM). Previous work suggests that flightin plays an essential, as yet undefined, role in normal sarcomere structure and contractile activity. Here we show that flightin is associated with thick filaments where it is likely to interact with the myosin rod. We have created a null mutation for flightin, fln0, that results in loss of flight ability but has no effect on fecundity or viability. Electron microscopy comparing pupa and adult fln0 IFM shows that sarcomeres, and thick and thin f

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11

Hao, Yudong, Sanford I. Bernstein, and Gerald H. Pollack. "Passive stiffness of Drosophila IFM myofibrils: a novel, high accuracy." Journal of Muscle Research and Cell Motility 25, no. 4-5 (2004): 359–66. http://dx.doi.org/10.1007/s10974-004-0684-5.

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12

Tanner, Bertrand C. W., Mark S. Miller, Becky M. Miller, et al. "COOH-terminal truncation of flightin decreases myofilament lattice organization, cross-bridge binding, and power output in Drosophila indirect flight muscle." American Journal of Physiology-Cell Physiology 301, no. 2 (2011): C383—C391. http://dx.doi.org/10.1152/ajpcell.00016.2011.

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The indirect flight muscle (IFM) of insects is characterized by a near crystalline myofilament lattice structure that likely evolved to achieve high power output. In Drosophila IFM, the myosin rod binding protein flightin plays a crucial role in thick filament organization and sarcomere integrity. Here we investigate the extent to which the COOH terminus of flightin contributes to IFM structure and mechanical performance using transgenic Drosophila expressing a truncated flightin lacking the 44 COOH-terminal amino acids ( flnΔ C44). Electron microscopy and X-ray diffraction measurements show d

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13

Dhanyasi, Nagaraju, Dagan Segal, Eyal Shimoni, et al. "Surface apposition and multiple cell contacts promote myoblast fusion in Drosophila flight muscles." Journal of Cell Biology 211, no. 1 (2015): 191–203. http://dx.doi.org/10.1083/jcb.201503005.

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Fusion of individual myoblasts to form multinucleated myofibers constitutes a widely conserved program for growth of the somatic musculature. We have used electron microscopy methods to study this key form of cell–cell fusion during development of the indirect flight muscles (IFMs) of Drosophila melanogaster. We find that IFM myoblast–myotube fusion proceeds in a stepwise fashion and is governed by apparent cross talk between transmembrane and cytoskeletal elements. Our analysis suggests that cell adhesion is necessary for bringing myoblasts to within a minimal distance from the myotubes. The

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14

Fernandes, J., M. Bate, and K. Vijayraghavan. "Development of the indirect flight muscles of Drosophila." Development 113, no. 1 (1991): 67–77. http://dx.doi.org/10.1242/dev.113.1.67.

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We have followed the pupal development of the indirect flight muscles (IFMs) of Drosophila melanogaster. At the onset of metamorphosis larval muscles start to histolyze, with the exception of a specific set of thoracic muscles. Myoblasts surround these persisting larval muscles and begin the formation of one group of adult indirect flight muscles, the dorsal longitudinal muscles. We show that the other group of indirect flight muscles, the dorsoventral muscles, develops simultaneously but without the use of larval templates. By morphological criteria and by patterns of specific gene expression

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15

Warmke, J. W., A. J. Kreuz, and S. Falkenthal. "Co-localization to chromosome bands 99E1-3 of the Drosophila melanogaster myosin light chain-2 gene and a haplo-insufficient locus that affects flight behavior." Genetics 122, no. 1 (1989): 139–51. http://dx.doi.org/10.1093/genetics/122.1.139.

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Abstract Using overlapping synthetic deficiencies, we find that a haplo-insufficient locus affecting flight behavior and the myosin light chain-2 gene co-map to the Drosophila melanogaster polytene chromosome interval 99D9-E1 to 99E2-3. From screening over 9000 EMS-treated chromosomes, we obtained alleles of two complementation groups that map to this same interval. One of these complementation groups lfm(3)99Eb, exhibits dominant flightless behavior; thus, flightless behavior of the deficiency is in all likelihood due to hemizygosity of this single locus. Rescue of flightless behavior by a du

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16

Brault, Véronique, Ursula Sauder, Mary C. Reedy, Ueli Aebi, and Cora-Ann Schoenenberger. "Differential Epitope Tagging of Actin in TransformedDrosophila Produces Distinct Effects on Myofibril Assembly and Function of the Indirect Flight Muscle." Molecular Biology of the Cell 10, no. 1 (1999): 135–49. http://dx.doi.org/10.1091/mbc.10.1.135.

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We have tested the impact of tags on the structure and function of indirect flight muscle (IFM)-specific Act88F actin by transforming mutant Drosophila melanogaster, which do not express endogenous actin in their IFMs, with tagged Act88F constructs. Epitope tagging is often the method of choice to monitor the fate of a protein when a specific antibody is not available. Studies addressing the functional significance of the closely related actin isoforms rely almost exclusively on tagged exogenous actin, because only few antibodies exist that can discriminate between isoforms. Thereby it is wide

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Standiford, David M., Wei Tao Sun, Mary Beth Davis, and Charles P. Emerson. "Positive and Negative Intronic Regulatory Elements Control Muscle-Specific Alternative Exon Splicing of Drosophila Myosin Heavy Chain Transcripts." Genetics 157, no. 1 (2001): 259–71. http://dx.doi.org/10.1093/genetics/157.1.259.

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Abstract Alternative splicing of Drosophila muscle myosin heavy chain (MHC) transcripts is precisely regulated to ensure the expression of specific MHC isoforms required for the distinctive contractile activities of physiologically specialized muscles. We have used transgenic expression analysis in combination with mutagenesis to identify cis-regulatory sequences that are required for muscle-specific splicing of exon 11, which is encoded by five alternative exons that produce alternative “converter” domains in the MHC head. Here, we report the identification of three conserved intronic element

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18

Tansey, T., J. R. Schultz, R. C. Miller, and R. V. Storti. "Small differences in Drosophila tropomyosin expression have significant effects on muscle function." Molecular and Cellular Biology 11, no. 12 (1991): 6337–42. http://dx.doi.org/10.1128/mcb.11.12.6337-6342.1991.

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The effects of promoter deletions on Drosophila tropomyosin I (TmI) gene expression have been determined by measuring TmI RNA levels in transformed flies. Decreases in RNA levels have been correlated with rescue of flightless and jumpless mutant phenotypes in Ifm(3)3 mutant transformed flies and changes in muscle ultrastructure. The results of this analysis have allowed us to identify a region responsible for 20% of maximal TmI expression, estimate threshold levels of TmI RNA required for indirect flight and jump muscle function, and obtain evidence suggesting that sarcomere length may be an i

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Tansey, T., J. R. Schultz, R. C. Miller, and R. V. Storti. "Small differences in Drosophila tropomyosin expression have significant effects on muscle function." Molecular and Cellular Biology 11, no. 12 (1991): 6337–42. http://dx.doi.org/10.1128/mcb.11.12.6337.

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The effects of promoter deletions on Drosophila tropomyosin I (TmI) gene expression have been determined by measuring TmI RNA levels in transformed flies. Decreases in RNA levels have been correlated with rescue of flightless and jumpless mutant phenotypes in Ifm(3)3 mutant transformed flies and changes in muscle ultrastructure. The results of this analysis have allowed us to identify a region responsible for 20% of maximal TmI expression, estimate threshold levels of TmI RNA required for indirect flight and jump muscle function, and obtain evidence suggesting that sarcomere length may be an i

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Schultz, J. R., T. Tansey, L. Gremke, and R. V. Storti. "A muscle-specific intron enhancer required for rescue of indirect flight muscle and jump muscle function regulates Drosophila tropomyosin I gene expression." Molecular and Cellular Biology 11, no. 4 (1991): 1901–11. http://dx.doi.org/10.1128/mcb.11.4.1901-1911.1991.

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The control of expression of the Drosophila melanogaster tropomyosin I (TmI) gene has been investigated by P-element transformation and rescue of the flightless and jumpless TmI mutant strain, Ifm(3)3. To localize cis-acting DNA sequences that control TmI gene expression, Ifm(3)3 flies were transformed with P-element plasmids containing various deletions and rearrangements of the TmI gene. The effects of these mutations on TmI gene expression were studied by analyzing both the extent of rescue of the Ifm(3)3 mutant phenotypes and determining TmI RNA levels in the transformed flies by primer ex

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Schultz, J. R., T. Tansey, L. Gremke, and R. V. Storti. "A muscle-specific intron enhancer required for rescue of indirect flight muscle and jump muscle function regulates Drosophila tropomyosin I gene expression." Molecular and Cellular Biology 11, no. 4 (1991): 1901–11. http://dx.doi.org/10.1128/mcb.11.4.1901.

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The control of expression of the Drosophila melanogaster tropomyosin I (TmI) gene has been investigated by P-element transformation and rescue of the flightless and jumpless TmI mutant strain, Ifm(3)3. To localize cis-acting DNA sequences that control TmI gene expression, Ifm(3)3 flies were transformed with P-element plasmids containing various deletions and rearrangements of the TmI gene. The effects of these mutations on TmI gene expression were studied by analyzing both the extent of rescue of the Ifm(3)3 mutant phenotypes and determining TmI RNA levels in the transformed flies by primer ex

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22

Newhard, Christopher S., Sam Walcott, and Douglas M. Swank. "The load dependence of muscle’s force-velocity curve is modulated by alternative myosin converter domains." American Journal of Physiology-Cell Physiology 316, no. 6 (2019): C844—C861. http://dx.doi.org/10.1152/ajpcell.00494.2018.

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The hyperbolic shape of the muscle force-velocity relationship (FVR) is characteristic of all muscle fiber types. The degree of curvature of the hyperbola varies between muscle fiber types and is thought to be set by force-dependent properties of different myosin isoforms. However, the structural elements in myosin and the mechanism that determines force dependence are unresolved. We tested our hypothesis that the myosin converter domain plays a critical role in the force-velocity relationship (FVR) mechanism. Drosophila contains a single myosin heavy chain gene with five converters encoded by

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Komlós, Marcell, Janka Szinyákovics, Gergő Falcsik, et al. "The Small-Molecule Enhancers of Autophagy AUTEN-67 and -99 Delay Ageing in Drosophila Striated Muscle Cells." International Journal of Molecular Sciences 24, no. 9 (2023): 8100. http://dx.doi.org/10.3390/ijms24098100.

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Background: Autophagy (cellular self-degradation) plays a major role in maintaining the functional integrity (homeostasis) of essentially all eukaryotic cells. During the process, superfluous and damaged cellular constituents are delivered into the lysosomal compartment for enzymatic degradation. In humans, age-related defects in autophagy have been linked to the incidence of various age-associated degenerative pathologies (e.g., cancer, neurodegenerative diseases, diabetes, tissue atrophy and fibrosis, and immune deficiency) and accelerated ageing. Muscle mass decreases at detectable levels a

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Hastings, G. A., and C. P. Emerson. "Myosin functional domains encoded by alternative exons are expressed in specific thoracic muscles of Drosophila." Journal of Cell Biology 114, no. 2 (1991): 263–76. http://dx.doi.org/10.1083/jcb.114.2.263.

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The Drosophila 36B muscle myosin heavy chain (MHC) gene has five sets of alternatively spliced exons that encode functionally important domains of the MHC protein and provide a combinatorial potential for expression of as many as 480 MHC isoforms. In this study, in situ hybridization analysis has been used to examine the complexity and muscle specificity of MHC isoform expression in the fibrillar indirect flight muscle (IFM), the tubular direct flight muscles (DFM) and tubular tergal depressor of the trochanter muscle (TDT), and the visceral esophageal muscle in the adult thorax. Our results s

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Nongthomba, Upendra, Mark Cummins, Samantha Clark, Jim O. Vigoreaux, and John C. Sparrow. "Suppression of Muscle Hypercontraction by Mutations in the Myosin Heavy Chain Gene of Drosophila melanogaster." Genetics 164, no. 1 (2003): 209–22. http://dx.doi.org/10.1093/genetics/164.1.209.

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Abstract The indirect flight muscles (IFM) of Drosophila melanogaster provide a good genetic system with which to investigate muscle function. Flight muscle contraction is regulated by both stretch and Ca2+-induced thin filament (actin + tropomyosin + troponin complex) activation. Some mutants in troponin-I (TnI) and troponin-T (TnT) genes cause a “hypercontraction” muscle phenotype, suggesting that this condition arises from defects in Ca2+ regulation and actomyosin-generated tension. We have tested the hypothesis that missense mutations of the myosin heavy chain gene, Mhc, which suppress the

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Menard, Lynda M., Neil B. Wood, and Jim O. Vigoreaux. "Contiguity and Structural Impacts of a Non-Myosin Protein within the Thick Filament Myosin Layers." Biology 10, no. 7 (2021): 613. http://dx.doi.org/10.3390/biology10070613.

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Myosin dimers arranged in layers and interspersed with non-myosin densities have been described by cryo-EM 3D reconstruction of the thick filament in Lethocerus at 5.5 Å resolution. One of the non-myosin densities, denoted the ‘red density’, is hypothesized to be flightin, an LMM-binding protein essential to the structure and function of Drosophila indirect flight muscle (IFM). Here, we build upon the 3D reconstruction results specific to the red density and its engagement with the myosin coiled-coil rods that form the backbone of the thick filament. Each independent red density winds its way

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Madan, Aditi, Divesh Thimmaiya, Ari Franco-Cea, et al. "Transcriptome analysis of IFM-specific actin and myosin nulls in Drosophila melanogaster unravels lesion-specific expression blueprints across muscle mutations." Gene 631 (October 2017): 16–28. http://dx.doi.org/10.1016/j.gene.2017.07.061.

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Chun, M., and S. Falkenthal. "Ifm(2)2 is a myosin heavy chain allele that disrupts myofibrillar assembly only in the indirect flight muscle of Drosophila melanogaster." Journal of Cell Biology 107, no. 6 (1988): 2613–21. http://dx.doi.org/10.1083/jcb.107.6.2613.

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Using a combination of molecular and genetic techniques we demonstrate that Ifm(2)2 is an allele of the single-copy sarcomeric myosin heavy chain gene. Flies homozygous for this allele accumulate wild-type levels of mRNA and protein in tubular muscle of adults, but fail to accumulate detectable amounts of myosin heavy chain mRNA or protein in the indirect flight muscle. We propose that the mutation interferes with either transcription of the gene or splicing of the primary transcript in the indirect flight muscle and not in other muscle tissues. Biochemical and electron microscopic analysis of

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Chakravorty, Samya, Bertrand C. W. Tanner, Veronica Lee Foelber, et al. "Flightin maintains myofilament lattice organization required for optimal flight power and courtship song quality in Drosophila." Proceedings of the Royal Society B: Biological Sciences 284, no. 1854 (2017): 20170431. http://dx.doi.org/10.1098/rspb.2017.0431.

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The indirect flight muscles (IFMs) of Drosophila and other insects with asynchronous flight muscles are characterized by a crystalline myofilament lattice structure. The high-order lattice regularity is considered an adaptation for enhanced power output, but supporting evidence for this claim is lacking. We show that IFMs from transgenic flies expressing flightin with a deletion of its poorly conserved N-terminal domain ( fln ΔN62 ) have reduced inter-thick filament spacing and a less regular lattice. This resulted in a decrease in flight ability by 33% and in skinned fibre oscillatory power o

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Cripps, R. M., E. Ball, M. Stark, A. Lawn, and J. C. Sparrow. "Recovery of dominant, autosomal flightless mutants of Drosophila melanogaster and identification of a new gene required for normal muscle structure and function." Genetics 137, no. 1 (1994): 151–64. http://dx.doi.org/10.1093/genetics/137.1.151.

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Abstract To identify further mutations affecting muscle function and development in Drosophila melanogaster we recovered 22 autosomal dominant flightless mutations. From these we have isolated eight viable and lethal alleles of the muscle myosin heavy chain gene, and seven viable alleles of the indirect flight muscle (IFM)-specific Act88F actin gene. The Mhc mutations display a variety of phenotypic effects, ranging from reductions in myosin heavy chain content in the indirect flight muscles only, to reductions in the levels of this protein in other muscles. The Act88F mutations range from tho

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Menard, Lynda M., Neil B. Wood, and Jim O. Vigoreaux. "Secondary Structure of the Novel Myosin Binding Domain WYR and Implications within Myosin Structure." Biology 10, no. 7 (2021): 603. http://dx.doi.org/10.3390/biology10070603.

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Structural changes in the myosin II light meromyosin (LMM) that influence thick filament mechanical properties and muscle function are modulated by LMM-binding proteins. Flightin is an LMM-binding protein indispensable for the function of Drosophila indirect flight muscle (IFM). Flightin has a three-domain structure that includes WYR, a novel 52 aa domain conserved throughout Pancrustacea. In this study, we (i) test the hypothesis that WYR binds the LMM, (ii) characterize the secondary structure of WYR, and (iii) examine the structural impact WYR has on the LMM. Circular dichroism at 260–190 n

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Walls, Stanley M., Dale A. Chatfield, Karen Ocorr, Greg L. Harris та Rolf Bodmer. "Systemic and heart autonomous effects of sphingosine Δ4 desaturase deficiency in lipotoxic cardiac pathophysiology". Disease Models & Mechanisms 13, № 8 (2020): dmm043083. http://dx.doi.org/10.1242/dmm.043083.

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ABSTRACTLipotoxic cardiomyopathy (LCM) is characterized by cardiac steatosis, including the accumulation of fatty acids, triglycerides and ceramides. Model systems have shown the inhibition of ceramide biosynthesis to antagonize obesity and improve insulin sensitivity. Sphingosine Δ4 desaturase (encoded by ifc in Drosophila melanogaster) enzymatically converts dihydroceramide into ceramide. Here, we examine ifc mutants to study the effects of desaturase deficiency on cardiac function in Drosophila. Interestingly, ifc mutants exhibited classic hallmarks of LCM: cardiac chamber dilation, contrac

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Bloemink, Marieke J., Karen H. Hsu, Michael A. Geeves, and Sanford I. Bernstein. "Alternative N-terminal regions of Drosophila myosin heavy chain II regulate communication of the purine binding loop with the essential light chain." Journal of Biological Chemistry 295, no. 42 (2020): 14522–35. http://dx.doi.org/10.1074/jbc.ra120.014684.

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We investigated the biochemical and biophysical properties of one of the four alternative exon-encoded regions within the Drosophila myosin catalytic domain. This region is encoded by alternative exons 3a and 3b and includes part of the N-terminal β-barrel. Chimeric myosin constructs (IFI-3a and EMB-3b) were generated by exchanging the exon 3–encoded areas between native slow embryonic body wall (EMB) and fast indirect flight muscle myosin isoforms (IFI). We found that this exchange alters the kinetic properties of the myosin S1 head. The ADP release rate (k-D) in the absence of actin is compl

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Wang, Yang, Girish C. Melkani, Jennifer A. Suggs, et al. "Expression of the inclusion body myopathy 3 mutation in Drosophila depresses myosin function and stability and recapitulates muscle inclusions and weakness." Molecular Biology of the Cell 23, no. 11 (2012): 2057–65. http://dx.doi.org/10.1091/mbc.e12-02-0120.

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Hereditary myosin myopathies are characterized by variable clinical features. Inclusion body myopathy 3 (IBM-3) is an autosomal dominant disease associated with a missense mutation (E706K) in the myosin heavy chain IIa gene. Adult patients experience progressive muscle weakness. Biopsies reveal dystrophic changes, rimmed vacuoles with cytoplasmic inclusions, and focal disorganization of myofilaments. We constructed a transgene encoding E706K myosin and expressed it in Drosophila (E701K) indirect flight and jump muscles to establish a novel homozygous organism with homogeneous populations of fa

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Littlefield, Kimberly Palmiter, Douglas M. Swank, Becky M. Sanchez, Aileen F. Knowles, David M. Warshaw, and Sanford I. Bernstein. "The converter domain modulates kinetic properties ofDrosophila myosin." American Journal of Physiology-Cell Physiology 284, no. 4 (2003): C1031—C1038. http://dx.doi.org/10.1152/ajpcell.00474.2002.

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Recently the converter domain, an integral part of the “mechanical element” common to all molecular motors, was proposed to modulate the kinetic properties of Drosophila chimeric myosin isoforms. Here we investigated the molecular basis of actin filament velocity ( V actin) changes previously observed with the chimeric EMB-IC and IFI-EC myosin proteins [the embryonic body wall muscle (EMB) and indirect flight muscle isoforms (IFI) with genetic substitution of the IFI and EMB converter domains, respectively]. In the laser trap assay the IFI and IFI-EC myosins generate the same unitary step disp

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Moshrefi, Mandana, Kamal Ahmadi, Amin Purhematy, Maziar Jajarmi, and yasin SarveAhrabi. "Detection of Antibacterial Properties of Musca domestica, Drosophila melanogaster, and Sarcophaga nodosa Using Resazurin as A Growth Indicator in Bacterial Cells." Infection Epidemiology and Microbiology 6, no. 3 (2020): 201–9. http://dx.doi.org/10.29252/iem.6.3.201.

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Lee, Pauline, Ngoc Ho, Terri Gelbart, and Ernest Beutler. "Polymorphisms in the human homologue of the drosophila Indy (I'm not dead yet) gene." Mechanisms of Ageing and Development 124, no. 8-9 (2003): 897–902. http://dx.doi.org/10.1016/s0047-6374(03)00149-0.

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Cormier, Sarah, Stéphanie Le Bras, Céline Souilhol, et al. "The Murine Ortholog of Notchless, a Direct Regulator of the Notch Pathway in Drosophila melanogaster, Is Essential for Survival of Inner Cell Mass Cells." Molecular and Cellular Biology 26, no. 9 (2006): 3541–49. http://dx.doi.org/10.1128/mcb.26.9.3541-3549.2006.

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ABSTRACT Notch signaling is an evolutionarily conserved pathway involved in intercellular communication and is essential for proper cell fate choices. Numerous genes participate in the modulation of the Notch signaling pathway activity. Among them, Notchless (Nle) is a direct regulator of the Notch activity identified in Drosophila melanogaster. Here, we characterized the murine ortholog of Nle and demonstrated that it has conserved the ability to modulate Notch signaling. We also generated mice deficient for mouse Nle (mNle) and showed that its disruption resulted in embryonic lethality short

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Zheng, Jolene, David Heber, Mingming Wang, et al. "Pomegranate juice and extract extended lifespan and reduced intestinal fat deposition in Caenorhabditis elegans." International Journal for Vitamin and Nutrition Research 87, no. 3-4 (2017): 149–58. http://dx.doi.org/10.1024/0300-9831/a000570.

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Abstract. Pomegranate juice with a high content of polyphenols, pomegranate extract, ellagic acid, and urolithin A, have anti-oxidant and anti-obesity effects in humans. Pomegranate juice extends lifespan of Drosophila melanogaster. Caenorhabditis elegans (C. elegans) (n = 6) compared to the control group in each treatment, lifespan was increased by pomegranate juice in wild type (N2, 56 %, P < 0.001) and daf-16 mutant (daf-16(mgDf50)I) (18 %, P = 0.00012), by pomegranate extract in N2 (28 %, P = 0.00004) and in daf-16(mgDf50)I (10 %, P < 0.05), or by ellagic acid (11 %, P < 0.05). Po

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INOUE, Katsuhisa, Lina ZHUANG, Dennis M. MADDOX, Sylvia B. SMITH, and Vadivel GANAPATHY. "Human sodium-coupled citrate transporter, the orthologue of Drosophila Indy, as a novel target for lithium action." Biochemical Journal 374, no. 1 (2003): 21–26. http://dx.doi.org/10.1042/bj20030827.

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NaCT (sodium-coupled citrate transporter) is an Na+-coupled citrate transporter identified recently in mammals that mediates the cellular uptake of citrate. It is expressed predominantly in the liver. NaCT is structurally and functionally related to the product of the Indy (I'm not dead yet) gene in Drosophila, the dysfunction of which leads to lifespan extension. Here, we show that NaCT mediates the utilization of extracellular citrate for fat synthesis in human liver cells, and that the process is stimulated by lithium. The transport function of NaCT is enhanced by lithium at concentrations

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Kopel, Jonathan J., Yangzom D. Bhutia, Sathish Sivaprakasam, and Vadivel Ganapathy. "Consequences of NaCT/SLC13A5/mINDY deficiency: good versus evil, separated only by the blood–brain barrier." Biochemical Journal 478, no. 3 (2021): 463–86. http://dx.doi.org/10.1042/bcj20200877.

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NaCT/SLC13A5 is a Na+-coupled transporter for citrate in hepatocytes, neurons, and testes. It is also called mINDY (mammalian ortholog of ‘I'm Not Dead Yet’ in Drosophila). Deletion of Slc13a5 in mice leads to an advantageous phenotype, protecting against diet-induced obesity, and diabetes. In contrast, loss-of-function mutations in SLC13A5 in humans cause a severe disease, EIEE25/DEE25 (early infantile epileptic encephalopathy-25/developmental epileptic encephalopathy-25). The difference between mice and humans in the consequences of the transporter deficiency is intriguing but probably expla

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Knauf, Felix, Nilufar Mohebbi, Carsten Teichert, et al. "The life-extending gene Indy encodes an exchanger for Krebs-cycle intermediates." Biochemical Journal 397, no. 1 (2006): 25–29. http://dx.doi.org/10.1042/bj20060409.

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A longevity gene called Indy (for ‘I'm not dead yet’), with similarity to mammalian genes encoding sodium–dicarboxylate cotransporters, was identified in Drosophila melanogaster. Functional studies in Xenopus oocytes showed that INDY mediates the flux of dicarboxylates and citrate across the plasma membrane, but the specific transport mechanism mediated by INDY was not identified. To test whether INDY functions as an anion exchanger, we examined whether substrate efflux is stimulated by transportable substrates added to the external medium. Efflux of [14C]citrate from INDY-expressing oocytes w

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Shwartz, Arkadi, Nagaraju Dhanyasi, Eyal D. Schejter, and Ben-Zion Shilo. "The Drosophila formin Fhos is a primary mediator of sarcomeric thin-filament array assembly." eLife 5 (October 12, 2016). http://dx.doi.org/10.7554/elife.16540.

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Actin-based thin filament arrays constitute a fundamental core component of muscle sarcomeres. We have used formation of the Drosophila indirect flight musculature for studying the assembly and maturation of thin-filament arrays in a skeletal muscle model system. Employing GFP-tagged actin monomer incorporation, we identify several distinct phases in the dynamic construction of thin-filament arrays. This sequence includes assembly of nascent arrays after an initial period of intensive microfilament synthesis, followed by array elongation, primarily from filament pointed-ends, radial growth of

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Gunderson, Jakob T., Ashley E. Peppriell, Ian N. Krout, Daria Vorojeikina, and Matthew D. Rand. "Neuroligin-1 is a mediator of methylmercury neuromuscular toxicity." Toxicological Sciences, September 21, 2021. http://dx.doi.org/10.1093/toxsci/kfab114.

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Abstract Methylmercury (MeHg) is a developmental toxicant capable of eliciting neurocognitive and neuromuscular deficits in children with in utero exposure. Previous research in Drosophila melanogaster uncovered that developmental MeHg exposure simultaneously targets the developing musculature and innervating motor neuron in the embryo, along with identifying Drosophila neuroligin 1 (nlg1) as a gene associated with developmental MeHg sensitivity. Nlg1 and its transsynaptic partner neurexin 1 (Nrx1) are critical for axonal arborization and NMJ maturation. We investigated the effects of MeHg exp

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Lin, Min-Han, Madeline K. Jensen, Nathan D. Elrod, et al. "Inositol hexakisphosphate is required for Integrator function." Nature Communications 13, no. 1 (2022). http://dx.doi.org/10.1038/s41467-022-33506-3.

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AbstractIntegrator is a multi-subunit protein complex associated with RNA polymerase II (Pol II), with critical roles in noncoding RNA 3′-end processing and transcription attenuation of a broad collection of mRNAs. IntS11 is the endonuclease for RNA cleavage, as a part of the IntS4-IntS9-IntS11 Integrator cleavage module (ICM). Here we report a cryo-EM structure of the Drosophila ICM, at 2.74 Å resolution, revealing stable association of an inositol hexakisphosphate (IP6) molecule. The IP6 binding site is located in a highly electropositive pocket at an interface among all three subunits of IC

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Naït-Saïdi, Rima, Aymeric Chartier, Emmanuelle Abgueguen, Philippe Guédat, and Martine Simonelig. "The small compound Icerguastat reduces muscle defects in oculopharyngeal muscular dystrophy through the PERK pathway of the unfolded protein response." Open Biology 13, no. 4 (2023). http://dx.doi.org/10.1098/rsob.230008.

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Oculopharyngeal muscular dystrophy (OPMD) is an autosomal dominant disease characterized by the progressive degeneration of specific muscles. OPMD is due to a mutation in the gene encoding poly(A) binding protein nuclear 1 (PABPN1) leading to a stretch of 11 to 18 alanines at N-terminus of the protein, instead of 10 alanines in the normal protein. This alanine tract extension induces the misfolding and aggregation of PABPN1 in muscle nuclei. Here, using Drosophila OPMD models, we show that the unfolded protein response (UPR) is activated in OPMD upon endoplasmic reticulum stress. Mutations in

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