scholarly journals Dystroglycan and Protein O-Mannosyltransferases 1 and 2 Are Required to Maintain Integrity of Drosophila Larval Muscles

2007 ◽  
Vol 18 (12) ◽  
pp. 4721-4730 ◽  
Author(s):  
Nicola Haines ◽  
Sara Seabrooke ◽  
Bryan A. Stewart
Keyword(s):  
Muscular Dystrophy ◽  
Muscle Contraction ◽  
Body Wall ◽  
Membrane Resistance ◽  
Muscle Membrane ◽  
Muscle Attachment ◽  
Larval Body ◽  
Genes Encoding ◽  
Body Wall Muscles ◽  
Drosophila Mutant

In vertebrates, mutations in Protein O-mannosyltransferase1 (POMT1) or POMT2 are associated with muscular dystrophy due to a requirement for O-linked mannose glycans on the Dystroglycan (Dg) protein. In this study we examine larval body wall muscles of Drosophila mutant for Dg, or RNA interference knockdown for Dg and find defects in muscle attachment, altered muscle contraction, and a change in muscle membrane resistance. To determine if POMTs are required for Dg function in Drosophila, we examine larvae mutant for genes encoding POMT1 or POMT2. Larvae mutant for either POMT, or doubly mutant for both, show muscle attachment and muscle contraction phenotypes identical to those associated with reduced Dg function, consistent with a requirement for O-linked mannose on Drosophila Dg. Together these data establish a central role for Dg in maintaining integrity in Drosophila larval muscles and demonstrate the importance of glycosylation to Dg function in Drosophila. This study opens the possibility of using Drosophila to investigate muscular dystrophy.

Electrophysiological Recording from Drosophila Larval Body-Wall Muscles

2010 ◽  
Vol 2010 (9) ◽  
pp. pdb.prot5487-pdb.prot5487 ◽  
Author(s):  
B. Zhang ◽  
B. Stewart
Keyword(s):  
Body Wall ◽  
Electrophysiological Recording ◽  
Larval Body ◽  
Body Wall Muscles

Development of Larval Body Wall Muscles

1999 ◽  
Vol 43 ◽  
pp. 25-44 ◽  
Author(s):  
M BATE ◽  
M LANDGRAF ◽  
M GOMEZBATE
Keyword(s):  
Body Wall ◽  
Larval Body ◽  
Body Wall Muscles

Dissection of Drosophila Larval Body-Wall Muscles

2010 ◽  
Vol 2010 (8) ◽  
pp. pdb.prot5469 ◽  
Author(s):  
Preethi Ramachandran ◽  
Vivian Budnik
Keyword(s):  
Body Wall ◽  
Larval Body ◽  
Body Wall Muscles

Immunocytochemical Staining of Drosophila Larval Body-Wall Muscles

2010 ◽  
Vol 2010 (8) ◽  
pp. pdb.prot5470 ◽  
Author(s):  
Preethi Ramachandran ◽  
Vivian Budnik
Keyword(s):  
Body Wall ◽  
Immunocytochemical Staining ◽  
Larval Body ◽  
Body Wall Muscles

scholarly journals Gelsolin and dCryAB act downstream of muscle identity genes and contribute to preventing muscle splitting and branching in Drosophila

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Benjamin Bertin ◽  
Yoan Renaud ◽  
Teresa Jagla ◽  
Guillaume Lavergne ◽  
Cristiana Dondi ◽  
...  
Keyword(s):  
Body Wall ◽  
Critical Role ◽  
Interacting Proteins ◽  
Cell Type ◽  
Larval Body ◽  
A Cell ◽  
Body Wall Muscles ◽  
Cell Type Specific ◽  
Muscle Types ◽  
Identify Gene Expression

AbstractA combinatorial code of identity transcription factors (iTFs) specifies the diversity of muscle types in Drosophila. We previously showed that two iTFs, Lms and Ap, play critical role in the identity of a subset of larval body wall muscles, the lateral transverse (LT) muscles. Intriguingly, a small portion of ap and lms mutants displays an increased number of LT muscles, a phenotype that recalls pathological split muscle fibers in human. However, genes acting downstream of Ap and Lms to prevent these aberrant muscle feature are not known. Here, we applied a cell type specific translational profiling (TRAP) to identify gene expression signatures underlying identity of muscle subsets including the LT muscles. We found that Gelsolin (Gel) and dCryAB, both encoding actin-interacting proteins, displayed LT muscle prevailing expression positively regulated by, the LT iTFs. Loss of dCryAB function resulted in LTs with irregular shape and occasional branched ends also observed in ap and lms mutant contexts. In contrast, enlarged and then split LTs with a greater number of myonuclei formed in Gel mutants while Gel gain of function resulted in unfused myoblasts, collectively indicating that Gel regulates LTs size and prevents splitting by limiting myoblast fusion. Thus, dCryAB and Gel act downstream of Lms and Ap and contribute to preventing LT muscle branching and splitting. Our findings offer first clues to still unknown mechanisms of pathological muscle splitting commonly detected in human dystrophic muscles and causing muscle weakness.

scholarly journals Maintenance of the K+ activity gradient in insect muscle compared in diptera and lepidoptera: contributions of metabolic and exchanger mechanisms

1996 ◽  
Vol 199 (8) ◽  
pp. 1857-1872
Author(s):  
E Fitzgerald ◽  
M Djamgoz ◽  
S Dunbar
Keyword(s):  
Body Wall ◽  
Specific Inhibitor ◽  
Input Resistance ◽  
The Body ◽  
Comparative Approach ◽  
Larval Body ◽  
Insect Muscle ◽  
Body Wall Muscles ◽  
K Transport ◽  
K Activity

Using a comparative approach, the mechanisms involved in maintenance of the transmembrane K+ activity gradients in the larval body-wall muscles of two insects, Phormia terraenovae (Diptera) and Spodoptera exigua (Lepidoptera), have been investigated. Double-barrelled K+-selective microelectrodes were used to obtain simultaneous measurements of intracellular K+ activity and membrane potential, whilst ordinary microelectrodes were used to monitor input resistance. By application of a variety of general metabolic blockers, the K+ gradients in both P. terraenovae and S. exigua muscle were found to be maintained, at least in part, by a metabolic component. Differences in sensitivity to dinitrophenol of the two insects suggested that the ATP-dependence of maintenance of the K+ gradient was significantly higher in P. terraenovae than in S. exigua. Vanadate sensitivity suggested that both insects possess P-type ATPases. The K+ activity gradient in P. terraenovae muscles was also found to be ouabain-sensitive, indicating the involvement of a Na+/K+-ATPase. In contrast, the K+ gradient in S. exigua muscles proved to be totally insensitive to ouabain but sensitive to amiloride. Application of the H+/K+-ATPase-specific inhibitor SCH 28080 suggested the presence of an H+/K+ pump similar to the mammalian gastric H+/K+-ATPase in the lepidopteran muscles. P. terraenovae muscles, however, were found to be totally insensitive to this inhibitor. Using the anion (Cl-)-dependent transport inhibitors bumetanide and SITS (4-acetamide-4-isothiocyanostilbene-2,2-disulphonic acid), P. terraenovae muscles were shown not to possess a Cl--dependent K+ transport mechanism. In contrast, a bumetanide-sensitive K+/Cl- cotransporter was likely to be involved in maintenance of the K+ gradient in S. exigua muscle. An additional SITS-sensitive Cl-/HCO3- exchanger could also have some indirect involvement in K+ maintenance through regulation of the inward Cl- gradient. The results are integrated in two ionic models, one for each insect, which could account for the bulk of K+ transport in the body-wall muscles of these insects.

scholarly journals Drosophila paramyosin is important for myoblast fusion and essential for myofibril formation

2003 ◽  
Vol 160 (6) ◽  
pp. 899-908 ◽  
Author(s):  
Hongjun Liu ◽  
Michelle Mardahl-Dumesnil ◽  
Sean T. Sweeney ◽  
Cahir J. O'Kane ◽  
Sanford I. Bernstein
Keyword(s):  
Muscle Contraction ◽  
Body Wall ◽  
Coiled Coil ◽  
Early Embryo ◽  
Myoblast Fusion ◽  
P Element ◽  
Structural Protein ◽  
Thick Filaments ◽  
Body Wall Muscles ◽  
Embryo Stage

Paramyosin is a major structural protein of thick filaments in invertebrate muscles. Coiled-coil dimers of paramyosin form a paracrystalline core of these filaments, and the motor protein myosin is arranged on the core surface. To investigate the function of paramyosin in myofibril assembly and muscle contraction, we functionally disrupted the Drosophila melanogaster paramyosin gene by mobilizing a P element located in its promoter region. Homozygous paramyosin mutants die at the late embryo stage. Mutants display defects in both myoblast fusion and in myofibril assembly in embryonic body wall muscles. Mutant embryos have an abnormal body wall muscle fiber pattern arising from defects in myoblast fusion. In addition, sarcomeric units do not assemble properly and muscle contractility is impaired. We confirmed that these defects are paramyosin-specific by rescuing the homozygous paramyosin mutant to adulthood with a paramyosin transgene. Antibody analysis of normal embryos demonstrated that paramyosin accumulates as a cytoplasmic protein in early embryo development before assembling into thick filaments. We conclude that paramyosin plays an unexpected role in myoblast fusion and is important for myofibril assembly and muscle contraction.

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