Drosophila Hsp67Bc hot-spot variants alter muscle structure and function

Cellular and Molecular Life Sciences : CMLS
Jadwiga JabłońskaMałgorzata Daczewska

Abstract

The Drosophila Hsp67Bc gene encodes a protein belonging to the small heat-shock protein (sHSP) family, identified as the nearest functional ortholog of human HSPB8. The most prominent activity of sHSPs is preventing the irreversible aggregation of various non-native polypeptides. Moreover, they are involved in processes such as development, aging, maintenance of the cytoskeletal architecture and autophagy. In larval muscles Hsp67Bc localizes to the Z- and A-bands, which suggests its role as part of the conserved chaperone complex required for Z-disk maintenance. In addition, Hsp67Bc is present at neuromuscular junctions (NMJs), which implies its involvement in the maintenance of NMJ structure. Here, we report the effects of muscle-target overexpression of Drosophila Hsp67Bc hot-spot variants Hsp67BcR126E and Hsp67BcR126N mimicking pathogenic variants of human HSPB8. Depending on the substitutions, we observed a different impact on muscle structure and performance. Expression of Hsp67BcR126E affects larval motility, which may be caused by impairment of mitochondrial respiratory function and/or by NMJ abnormalities manifested by a decrease in the number of synaptic boutons. In contrast, Hsp67BcR126N appears to be an aggregate-pro...Continue Reading

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Citations

Feb 26, 2020·International Journal of Molecular Sciences·Jaakko SarparantaBjarne Udd
Nov 8, 2018·International Journal of Molecular Sciences·Teresa JaglaKrzysztof Jagla
Jul 8, 2020·Cells·Preethi Poovathumkadavil, Krzysztof Jagla
Nov 1, 2021·Cell Biology International·Dina MalkeyevaSvetlana A Fedorova

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Methods Mentioned

BETA
PCR
transgenic
motility tests
dissection

Software Mentioned

FV10
_ Viewer
ImageJ
Olympus FV1000
Image J
ASW

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