Heat shock response inDrosophila

Pauli, Daniel; Arrigo, André‐Patrick; Tissières, A.

doi:10.1007/bf02118306

Cited by 66 publications

(41 citation statements)

References 101 publications

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“…It is known that high temperatures induce stress responses in flies, such as expression of HS proteins (56). Flies were reared under three conditions, including 1) room temperature (19 -23°C; designated as RT), 2) HS treatment (reared at 29 -30°C for 2-3 days prior to recording, designated as HS), and 3) post-HS treatment (reared at 29 -30°C for 2 days, followed by RT for 1 day prior to recording; designated as post-HS).…”

Section: Resultsmentioning

confidence: 99%

Differential behavioral state-dependence in the burst properties of CA3 and CA1 neurons

et al. 2006

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It has been shown that presenilin is involved in maintaining Ca 2؉ homeostasis in neurons, including regulating endoplasmic reticulum (ER) Ca 2؉ storage. From studies of primary cultures and cell lines, however, its role in stress-induced responses is still controversial. In the present study we analyzed the effects of presenilin mutations on membrane currents and synaptic functions in response to stress using an in vivo preparation. We examined voltage-gated K ؉ and Ca 2؉ currents at the Drosophila larval neuromuscular junction (NMJ) with voltage-clamp recordings. Our data showed that both currents were generally unaffected by loss-of-function or Alzheimer's disease (AD) -associated presenilin mutations under normal or stress conditions induced by heat shock (HS) or ER stress. In larvae expressing the mutant presenilins, prolonged Ca 2؉ tail current, reflecting slower deactivation kinetics of Ca 2؉ channels, was observed 1 day after stress treatments were terminated. It was further demonstrated that the L-type Ca 2؉ channel was specifically affected under these conditions. Moreover, synaptic plasticity at the NMJ was reduced in larvae expressing the mutant presenilins. At the behavioral level, memory in adult flies was impaired in the presenilin mutants 1 day after HS. The results show that presenilin function is important during the poststress period and its impairment contributes to memory dysfunction observed during adaptation to normal conditions after stress. Our findings suggest a new stress-related mechanism by which presenilin may be implicated in the neuropathology of

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Section: Resultsmentioning

confidence: 99%

Differential behavioral state-dependence in the burst properties of CA3 and CA1 neurons

et al. 2006

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“…The distinctive feature of the heat-shock response is the synthesis of a set of conserved heat-shock proteins (Hsp's;Lindquist 1986;Lindquist and Craig 1988;Parsell and Lindquist 1993;Feder and Hofmann 1999). Hsp's can protect against a number of cellular stresses, including high temperatures, oxidative stress, and a variety of cytotoxins (Craig 1985;Lindquist 1986;Bond and Schlesinger 1987;Pauli et al 1992;De Maio 1995;Morimoto et al 1997;Feder and Hofmann 1999;Jaattela 1999;Kregel 2002). Convincing evidence for the protective function of Hsp's is derived from the induced thermotolerance test.…”

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confidence: 99%

Loss of Hsp70 in Drosophila Is Pleiotropic, With Effects on Thermotolerance, Recovery From Heat Shock and Neurodegeneration

Gong

Golic²

2006

Genetics

128

106

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The heat-shock response is a programmed change in gene expression carried out by cells in response to environmental stress, such as heat. This response is universal and is characterized by the synthesis of a small group of conserved protein chaperones. In Drosophila melanogaster the Hsp70 chaperone dominates the profile of protein synthesis during the heat-shock response. We recently generated precise deletion alleles of the Hsp70 genes of D. melanogaster and have used those alleles to characterize the phenotypes of Hsp70-deficient flies. Flies with Hsp70 deletions have reduced thermotolerance. We find that Hsp70 is essential to survive a severe heat shock, but is not required to survive a milder heat shock, indicating that a significant degree of thermotolerance remains in the absence of Hsp70. However, flies without Hsp70 have a lengthened heat-shock response and an extended developmental delay after a non-lethal heat shock, indicating Hsp70 has an important role in recovery from stress, even at lower temperatures. Lack of Hsp70 also confers enhanced sensitivity to a temperature-sensitive lethal mutation and to the neurodegenerative effects produced by expression of a human polyglutamine disease protein.

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“…The heat shock response of Drosophila melanogaster is an ideal system for studying the processes of transcription activation and repression (6,35). During heat shock, the transcription and translation of gene products cease, accompanied by the extremely rapid induction of the heat shock genes (27,30,41).…”

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confidence: 99%

Protein Phosphatase 2A Activity Affects Histone H3 Phosphorylation and Transcription in Drosophila melanogaster

Nowak

Pai

Corcés

2003

Molecular and Cellular Biology

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Transcriptional activation of the heat shock genes during the heat shock response in Drosophila has been intimately linked to phosphorylation of histone H3 at serine 10, whereas repression of non-heat-shock genes correlates with dephosphorylation of histone H3. It is then possible that specific kinase and/or phosphatase activities may regulate histone phosphorylation and therefore transcription activation and repression, respectively. We find that treatment of cells with strong phosphatase inhibitors interferes with the genome-wide dephosphorylation of histone H3 normally observed at non-heat-shock genes during heat shock. Mutants in protein phosphatase type 2A (PP2A) also display reduced genome-wide H3 dephosphorylation, and sites of H3 phosphorylation that do not contain heat shock genes remain transcriptionally active during heat shock in PP2A mutants. Finally, the SET protein, a potent and highly selective inhibitor of PP2A activity that inhibits PP2A-mediated dephosphorylation of Ser10-phosphorylated H3, is detected at transcriptionally active regions of polytene chromosomes. These results suggest that activation and repression of gene expression during heat shock might be regulated by changes in PP2A activity controlled by the SET protein.

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Heat shock response inDrosophila

Cited by 66 publications

References 101 publications

Differential behavioral state-dependence in the burst properties of CA3 and CA1 neurons

Differential behavioral state-dependence in the burst properties of CA3 and CA1 neurons

Loss of Hsp70 in Drosophila Is Pleiotropic, With Effects on Thermotolerance, Recovery From Heat Shock and Neurodegeneration

Protein Phosphatase 2A Activity Affects Histone H3 Phosphorylation and Transcription in Drosophila melanogaster

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