Abstract
Using Drosophila muscle development as a model system makes possible the identification of genetic pathways, temporal regulation of development, mechanisms of cellular development, and physiological impacts in a single system. Here we describe the basic techniques for the evaluation of the cellular development of muscle in Drosophila in both embryos and in larvae. These techniques are discussed within the context of how the LINC complex contributes to muscle development.
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References
Chang W, Worman HJ, Gundersen GG (2015) Accessorizing and anchoring the LINC complex for multifunctionality. J Cell Biol 208:11–22. https://doi.org/10.1083/jcb.201409047
Meinke P, Nguyen TD, Wehnert MS (2011) The LINC complex and human disease. Biochem Soc Trans 39:1693–1697. https://doi.org/10.1042/BST20110658
Meinke P, Schirmer EC (2015) LINC’ing form and function at the nuclear envelope. FEBS Lett 589:2514–2521. https://doi.org/10.1016/j.febslet.2015.06.011
Luxton GWG, Gomes ER, Folker ES et al (2010) Linear arrays of nuclear envelope proteins harness retrograde actin flow for nuclear movement. Science 329:956–959. https://doi.org/10.1126/science.1189072
King MC, Drivas TG, Blobel G (2008) A network of nuclear envelope membrane proteins linking centromeres to microtubules. Cell 134:427–438
Zhang X, Lei K, Yuan X et al (2009) SUN1/2 and Syne/Nesprin-1/2 complexes connect centrosome to the nucleus during neurogenesis and neuronal migration in mice. Neuron 64:173–187. https://doi.org/10.1016/j.neuron.2009.08.018
Elhanany-Tamir H, Yu YV, Shnayder M et al (2012) Organelle positioning in muscles requires cooperation between two KASH proteins and microtubules. J Cell Biol 198:833–846. https://doi.org/10.1083/jcb.201204102
Zhang Q, Bethmann C, Worth NF et al (2007) Nesprin-1 and -2 are involved in the pathogenesis of Emery Dreifuss muscular dystrophy and are critical for nuclear envelope integrity. Hum Mol Genet 16:2816–2833. https://doi.org/10.1093/hmg/ddm238
Nagano A, Koga R, Ogawa M et al (1996) Emerin deficiency at the nuclear membrane in patients with Emery-Dreifuss muscular dystrophy. Nat Genet 12:254–259. https://doi.org/10.1038/ng0396-254
Bonne G, Di Barletta MR, Varnous S et al (1999) Mutations in the gene encoding lamin A/C cause autosomal dominant Emery-Dreifuss muscular dystrophy. Nat Genet 21:285–288. https://doi.org/10.1038/6799
Puckelwartz MJ, Kessler E, Zhang Y et al (2009) Disruption of nesprin-1 produces an Emery Dreifuss muscular dystrophy-like phenotype in mice. Hum Mol Genet 18:607–620. https://doi.org/10.1093/hmg/ddn386
Bione S, Maestrini E, Rivella S et al (1994) Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy. Nat Genet 8:323–327. https://doi.org/10.1038/ng1294-323
Wilson MH, Holzbaur ELF (2012) Opposing microtubule motors drive robust nuclear dynamics in developing muscle cells. J Cell Sci 125:4158–4169. https://doi.org/10.1242/jcs.108688
Cadot B, Gache V, Vasyutina E et al (2012) Nuclear movement during myotube formation is microtubule and dynein dependent and is regulated by Cdc42, Par6 and Par3. Nat Publ Group 13:741–749. https://doi.org/10.1038/embor.2012.89
Iyer SR, Shah SB, Valencia AP et al (2016) Altered nuclear dynamics in MDX myofibers. J Appl Physiol 122:470–481. https://doi.org/10.1152/japplphysiol.00857.2016
Oddoux S, Zaal KJ, Tate V et al (2013) Microtubules that form the stationary lattice of muscle fibers are dynamic and nucleated at Golgi elements. J Cell Biol 203:205–213. https://doi.org/10.1083/jcb.201304063
Metzger T, Gache V, Xu M et al (2012) MAP and kinesin-dependent nuclear positioning is required for skeletal muscle function. Nature 484:120–124. https://doi.org/10.1038/nature10914
Folker ES, Schulman VK, Baylies MK (2012) Muscle length and myonuclear position are independently regulated by distinct Dynein pathways. Development 139:3827–3837. https://doi.org/10.1242/dev.079178
Folker ES, Schulman VK, Baylies MK (2014) Translocating myonuclei have distinct leading and lagging edges that require kinesin and dynein. Development 141:355–366. https://doi.org/10.1242/dev.095612
Auld AL, Folker ES (2016) Nucleus-dependent sarcomere assembly is mediated by the LINC complex. Mol Biol Cell 27:2351–2359. https://doi.org/10.1091/mbc.E16-01-0021
Collins MA, Mandigo TR, Camuglia JM et al (2017) Emery-Dreifuss muscular dystrophy-linked genes and centronuclear myopathy-linked genes regulate myonuclear movement by distinct mechanisms. Mol Biol Cell. https://doi.org/10.1091/mbc.E16-10-0721
Richardson BE, Becket K, Nowak SJ, Baylies MK (2007) SCAR/WAVE and Arp2/3 are crucial for cytoskeletal remodeling at the site of myoblast fusion. Deveolpment 134: 4357-67. https://doi.org/10.1242/dev.010678
Barton LJ, Pinto BS, Wallrath LL, and Geyer PK (2016) The Drosophila nuclear lamina protein otefin is required fro germline stem cell survival. Dev Cell 25: 645-54. https://doi.org/10.1016/j.devcel.2013.05.023
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Auld, A.L., Collins, M.A., Mandigo, T.R., Folker, E.S. (2018). High-Resolution Imaging Methods to Analyze LINC Complex Function During Drosophila Muscle Development. In: Gundersen, G., Worman, H. (eds) The LINC Complex. Methods in Molecular Biology, vol 1840. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-8691-0_14
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