Integrin-mediated adhesion maintains sarcomeric integrity

Perkins, Alexander; Ellis, Stephanie J.; Asghari, Parisa; Shamsian, Arash; Moore, Edwin D.W.; Tanentzapf, Guy

doi:10.1016/j.ydbio.2009.10.034

Cited by 45 publications

(49 citation statements)

References 43 publications

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“…Climbing ability was assessed as described by Perkins et al (2010) using a modified form of the geotaxis assay (Leal and Neckameyer, 2002). Groups of 10 flies were placed in an empty vial at 29°C.…”

Section: Geotaxis (Climbing) Assaysmentioning

confidence: 99%

Integration of Taste and Calorie Sensing inDrosophila

et al. 2012

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Animals use gustatory information to assess the suitability of potential food sources and make critical decisions on what to consume. For example, the taste of sugar generally signals a potent dietary source of carbohydrates. However, the intensity of the sensory response to a particular sugar, or "sweetness," is not always a faithful reporter of its nutritional value, and recent evidence suggests that animals can sense the caloric content of food independently of taste. Here, we demonstrate that the vinegar fly Drosophila melanogaster uses both taste and calorie sensing to determine feeding choices, and that the relative contribution of each changes over time. Using the capillary feeder assay, we allowed flies to choose between sources of sugars that varied in their ratio of sweetness to caloric value. We found that flies initially consume sugars according to taste. However, over several hours their preference shifts toward the food source with higher caloric content. This behavioral shift occurs more rapidly following food deprivation and is modulated by cAMP and insulin signaling within neurons. Our results are consistent with the existence of a taste-independent calorie sensor in flies, and suggest that calorie-based reward modifies long-term feeding preferences.

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Section: Geotaxis (Climbing) Assaysmentioning

confidence: 99%

Integration of Taste and Calorie Sensing inDrosophila

et al. 2012

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“…Here, we extend the muscle analysis to the level of the sarcomere (Perkins et al, 2010;Schnorrer et al, 2010). Two titinlike proteins, Projectin and Kettin (Sallimus -FlyBase), form the connecting filaments in indirect flight muscles (IFMs) that link the Z-bands to thick filaments and function in muscle elasticity during oscillatory work in flight (Lakey et al, 1990;Moore et al, 1999;Ayme-Southgate et al, 2005;Bullard et al, 2006).…”

Section: Establishment Of a Dystrophic Myofibril Phenotypementioning

confidence: 99%

Genetic elevation of Sphingosine 1-phosphate suppresses dystrophic muscle phenotypes in Drosophila

et al. 2013

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SUMMARYDuchenne muscular dystrophy is a lethal genetic disease characterized by the loss of muscle integrity and function over time. Using Drosophila, we show that dystrophic muscle phenotypes can be significantly suppressed by a reduction of wunen, a homolog of lipid phosphate phosphatase 3, which in higher animals can dephosphorylate a range of phospholipids. Our suppression analyses include assessing the localization of Projectin protein, a titin homolog, in sarcomeres as well as muscle morphology and functional movement assays. We hypothesize that wunen-based suppression is through the elevation of the bioactive lipid Sphingosine 1-phosphate (S1P), which promotes cell proliferation and differentiation in many tissues, including muscle. We confirm the role of S1P in suppression by genetically altering S1P levels via reduction of S1P lyase (Sply) and by upregulating the serine palmitoyl-CoA transferase catalytic subunit gene lace, the first gene in the de novo sphingolipid biosynthetic pathway and find that these manipulations also reduce muscle degeneration. Furthermore, we show that reduction of spinster (which encodes a major facilitator family transporter, homologs of which in higher animals have been shown to transport S1P) can also suppress dystrophic muscle degeneration. Finally, administration to adult flies of pharmacological agents reported to elevate S1P signaling significantly suppresses dystrophic muscle phenotypes. Our data suggest that localized intracellular S1P elevation promotes the suppression of muscle wasting in flies.

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“…The following stocks were used: Df(2R)Exel6068, Mi{ET1} (Nguyen et al, 2007); abba , abba and abba (all from this study); mlp84B PD8-95 (similar to mlp84B P8 allele but without the original P-element; provided by K. Clark, University of Utah); Kettin protein trap line ZCL2144 [provided by L. Cooley, Yale University (Morin et al, 2001)]; UAS-abba RNAi lines (transformant ID 19290 and 19291; Vienna Drosophila RNAi Center); mef2-Gal4 [obtained from Bloomington Stock Center (Ranganayakulu et al, 1996)]; P{tubP-Gal80 ts }9;; mef2-Gal4 [provided by G. Tanentzapf, University of British Columbia, Canada (Perkins et al, 2010)]. All mutations were maintained over twi .eGFP balancers.…”

Section: Drosophila Stocksmentioning

confidence: 99%

Abba is an essential TRIM/RBCC protein for maintaining the integrity of sarcomeric cytoarchitecture

Domsch

Ezzeddine

Nguyen

2013

Journal of Cell Science

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SummaryOrganized sarcomeric striations are an evolutionarily conserved hallmark of functional skeletal muscles. Here, we demonstrate that the Drosophila Abba protein, a member of the TRIM/RBCC superfamily, has a pivotal regulatory role in maintaining proper sarcomeric cytoarchitecture during development and muscle usage. abba mutant embryos initially form muscles, but F-actin and Myosin striations become progressively disrupted when the muscles undergo growth and endure increased contractile forces during larval development. Abnormal Myosin aggregates and myofiber atrophy are also notable in the abba mutants. The larval defects result in compromised muscle function, and hence important morphogenetic events do not occur properly during pupation, leading to lethality. Abba is localized at larval Z-discs, and genetic evidence indicates that abba interacts with a-actinin, kettin/D-titin and mlp84B, genes that encode important Z-disc proteins for stable myofibrillar organization and optimal muscle function. RNAi experiments and ultrastructural analysis reveal that Abba has an additional crucial role in sarcomere maintenance in adult muscles. Abba is required to ensure the integrity and function of Z-discs and M-lines. Rescue experiments further show that Abba function is dependent upon its B-box/coiledcoil domain, NHL repeats and RING finger domain. The importance of these presumed protein-protein interactions and ubiquitin ligaseassociated domains supports our hypothesis that Abba is needed for specific protein complex formation and stabilization at Z-discs and M-lines.

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Integrin-mediated adhesion maintains sarcomeric integrity

Cited by 45 publications

References 43 publications

Integration of Taste and Calorie Sensing inDrosophila

Integration of Taste and Calorie Sensing inDrosophila

Genetic elevation of Sphingosine 1-phosphate suppresses dystrophic muscle phenotypes in Drosophila

Abba is an essential TRIM/RBCC protein for maintaining the integrity of sarcomeric cytoarchitecture

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