Аннотация:Key words: Drosophila melanogaster, Hsp70, mitochondria Motivation and Aim: Aging is associated with changes in many cellular functions, including a decrease in mitochondria function in skeletal muscles. Сhaperones regulate proteostasis, controlling protein refolding and nonspecific aggregation. We aimed to investigate the role of chaperones of the Hsp70 family in age-related changes in skeletal muscle proteome in D. melanogaster. Methods: Males of the D. melanogaster Hsp70-(Df(3R)Hsp70A,Df(3R)Hsp70B),strain with knockout of 6 genes from the Hsp70 family, were used in the study, as well as males of the control parent strain w1118. General functional status of flies was assessed during the life by vertical climbing speed. Fly's legs were prepared to evaluate genotype- and age-related changes in the proteome of skeletal muscles using shotgun quantitative (with isobaric labeling) proteomic. Results: There were no differences in survival between strains. Young Hsp70-flies show 2 times lower climbing speed compared to w1118. During aging only w1118 showed a decrease in the climbing speed, while the climbing speed of Hsp70-flies remained at a constant (and substantially reduced) level compare to the control. We detected 725 highly abundant proteins in skeletal muscle: the content of 67 and 88 proteins was reduced and increased respectively, in old Hsp70-compared to the age-matched control. Conclusion: Knockout of Hsp70 family genes does not affect lifespan, but reduces locomotor activity and down regulates proteins associates with carbohydrate metabolism and oxidation-reduction processes, in particular, with pentose phosphate pathway and cytochrome c oxidase. Acknowledgements: The study was supported by the Russian Science Foundation (grant 21-15-00405).