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Citation
Zatsepina, O.G., Nikitina, E.A., Shilova, V.Y., Chuvakova, L.N., Sorokina, S., Vorontsova, J.E., Tokmacheva, E.V., Funikov, S.Y., Rezvykh, A.P., Evgen'ev, M.B. (2021). Hsp70 affects memory formation and behaviorally relevant gene expression in Drosophila melanogaster.  Cell Stress Chaperones 26(3): 575--594.
FlyBase ID
FBrf0248901
Publication Type
Research paper
Abstract
Heat shock proteins, in particular Hsp70, play a central role in proteostasis in eukaryotic cells. Due to its chaperone properties, Hsp70 is involved in various processes after stress and under normal physiological conditions. In contrast to mammals and many Diptera species, inducible members of the Hsp70 family in Drosophila are constitutively synthesized at a low level and undergo dramatic induction after temperature elevation or other forms of stress. In the courtship suppression paradigm used in this study, Drosophila males that have been repeatedly rejected by mated females during courtship are less likely than naive males to court other females. Although numerous genes with known function were identified to play important roles in long-term memory, there is, to the best of our knowledge, no direct evidence implicating Hsp70 in this process. To elucidate a possible role of Hsp70 in memory formation, we used D. melanogaster strains containing different hsp70 copy numbers, including strains carrying a deletion of all six hsp70 genes. Our investigations exploring the memory of courtship rejection paradigm demonstrated that a low constitutive level of Hsp70 is apparently required for learning and the formation of short and long-term memories in males. The performed transcriptomic studies demonstrate that males with different hsp70 copy numbers differ significantly in the expression of a few definite groups of genes involved in mating, reproduction, and immunity in response to rejection. Specifically, our analysis reveals several major pathways that depend on the presence of hsp70 in the genome and participate in memory formation and consolidation, including the cAMP signaling cascade.
PubMed ID
PubMed Central ID
PMC8065088 (PMC) (EuropePMC)
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Secondary IDs
    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    Cell Stress Chaperones
    Title
    Cell Stress & Chaperones
    Publication Year
    1996-
    ISBN/ISSN
    1355-8145
    Data From Reference
    Aberrations (2)
    Alleles (2)
    Genes (6)
    Natural transposons (1)
    Insertions (1)
    Transgenic Constructs (1)