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IMMUNOFLUROESCENCE MICROSCOPY OF DROSOPHILA LARVAE IN THE NEUROMUSCULAR JUNCTION AND SEGMENTAL MUSCLES **

Abstract

Dynamin was initially identified in bovine brain tissue as a 100-kDa microtubule-binding protein sensitive to nucleotides. Studies of the temperature-sensitive Drosophila melanogaster mutant shibire revealed its essential role in membrane fission during synaptic vesicle recycling, as the mutant becomes paralyzed at restrictive temperatures because vesicle recycling is disrupted. Shibire was later shown to be the Drosophila homolog of dynamin. Dynamin acts as a GTPase “molecular scissor,” mediating vesicle release by severing the neck of budding vesicles during the late stage of clathrin-mediated endocytosis. Whereas Drosophila contains a single dynamin gene, humans express three isoforms that share strong sequence similarity but display distinct tissue distributions. Mutations in these genes have been linked to several human disorders, including Charcot-Marie-Tooth disease, centronuclear myopathy, and developmental epileptic encephalopathies. These findings emphasize the specialized functions of individual dynamin isoforms and their links to human disease. However, the tissue-specific mechanisms of these isoforms remain poorly understood. To address this gap, we will use Drosophila as an in vivo model. Drosophila has been proven to be an excellent model organism due to its genetic tractability, short generation time, low maintenance cost, and strong evolutionary conservation with humans. We are going to perform phenotypic analyses of third-instar larvae carrying disease-associated mutations, focusing on neuromuscular junction structure and muscle morphology using immunofluorescence microscopy. This work aims to elucidate the roles of dynamin in neural and muscular tissues, contributing to the advancement of targeted therapeutic strategies.

Acknowledgements

UNG Presidential Semester Award

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