Developmental Expression and Functions of the Small Heat Shock Proteins in Drosophila

Jagla, Teresa; Dubińska–Magiera, Magda; Poovathumkadavil, Preethi; Daczewska, Małgorzata; Jagla, Krzysztof

doi:10.3390/ijms19113441

Cited by 31 publications

(37 citation statements)

References 47 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…HSPs are molecular chaperones that represent an intracellular protein quality system to maintain cellular protein homeostasis, preventing aggregation and promoting protein de novo folding or refolding and degradation of misfolded proteins [8]. In addition, HSPs participate in developmental functions in a stress-independent manner [9,10]. In Drosophila development small Heat Shock proteins (sHsps) have a specific temporal and spatial pattern of expression [10].…”

Section: Introductionmentioning

confidence: 99%

Small heat shock proteins determine synapse number and neuronal activity during development

2020

View full text Add to dashboard Cite

Environmental changes cause stress, Reactive Oxygen Species and unfolded protein accumulation which hamper synaptic activity and trigger cell death. Heat shock proteins (HSPs) assist protein refolding to maintain proteostasis and cellular integrity. Mechanisms regulating the activity of HSPs include transcription factors and posttranslational modifications that ensure a rapid response. HSPs preserve synaptic function in the nervous system upon environmental insults or pathological factors and contribute to the coupling between environmental cues and neuron control of development. We have performed a biased screening in Drosophila melanogaster searching for synaptogenic modulators among HSPs during development. We explore the role of two small-HSPs (sHSPs), sHSP23 and sHSP26 in synaptogenesis and neuronal activity. Both sHSPs immunoprecipitate together and the equilibrium between both chaperones is required for neuronal development and activity. The molecular mechanism controlling HSP23 and HSP26 accumulation in neurons relies on a novel gene (CG1561), which we name Pinkman (pkm). We propose that sHSPs and Pkm are targets to modulate the impact of stress in neurons and to prevent synapse loss.

show abstract

Section: Introductionmentioning

confidence: 99%

Small heat shock proteins determine synapse number and neuronal activity during development

2020

View full text Add to dashboard Cite

show abstract

“…HSPs are molecular chaperones that represent an intracellular protein quality system to maintain cellular protein homeostasis (proteostasis), preventing aggregation and promoting protein de novo folding or refolding and degradation of misfolded proteins [8]. In addition, HSPs participate in developmental functions in a stress-independent manner [9,10]. In Drosophiladevelopment small Heat Shock proteins (sHsps) have a specific temporal and spatial pattern of expression [10].…”

Section: Introductionmentioning

confidence: 99%

“…In addition, HSPs participate in developmental functions in a stress-independent manner [9,10]. In Drosophiladevelopment small Heat Shock proteins (sHsps) have a specific temporal and spatial pattern of expression [10].…”

Section: Introductionmentioning

confidence: 99%

“…In particular, sHsp23 and sHsp26 show high expression levels in CNS during development, suggesting a role in neural development [10].…”

Section: Introductionmentioning

confidence: 99%

“…Here, we study the contribution of two sHsps, sHp23 and sHsp26 in the development of the CNS and synapse modulation. sHsp23 and sHsp26 are expressed in the CNS during the development [10,34,35] but their function remains unclear. In addition, we describe the function of CG1561, named Pinkman (Pkm), as a novel putative kinase that interacts with sHSP23 and sHSP26.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Small heat shock proteins determine synapse number and neuronal activity during development

Reyes

Santana

Casas‐Tintó

2020

Preprint

View full text Add to dashboard Cite

Environmental changes cause stress, Reactive Oxygen Species and unfolded protein accumulation which hamper synaptic activity and trigger cell death. Heat shock proteins (HSPs) assist protein refolding to maintain proteostasis and cellular integrity.Mechanisms regulating the activity of HSPs include transcription factors and posttranslational modifications that ensure a rapid response. HSPs preserve synaptic function in the nervous system upon environmental insults or pathological factors and contribute to the coupling between environmental cues and neuron control of development. We have performed a biased screening in Drosophilamelanogaster searching for synaptogenic modulators among HSPs during development. We explore the role of two small-HSPs (sHSPs), sHSP23 and sHSP26 in synaptogenesis and neuronal activity. Both sHSPs immunoprecipitate together and the equilibrium between both chaperones is required for neuronal development and activity. The molecular mechanism controlling HSP23 and HSP26 accumulation in neurons relies on a novel gene (CG1561), which we name Pinkman (pkm). We propose that sHSPs and Pkm are targets to modulate the impact of stress in neurons and to prevent synapse loss.

show abstract

Molecular chaperone HspB2 inhibited pancreatic cancer cell proliferation via activating p53 downstream gene RPRM, BAI1, and TSAP6

Wang

Fang

et al. 2019

J of Cellular Biochemistry

View full text Add to dashboard Cite

Heat shock proteins (HSPs) were known as the molecular chaperones, which play a pivotal role in the protein quality control system, ensuring correct folding of proteins, and facilitating the correct refolding of damaged proteins via the transient interaction with their substrate proteins. They also practice in the regulation of cell cycles and are involved in apoptosis. We found that HspB2 was almost completely silent in pancreatic cancer and few studies investigated the role of HspB2 in cancer cells, particularly in pancreatic cancer. Here, we reported that HspB2 effectively inhibited cell proliferation in Panc-1 cells. Specifically, we demonstrated that HspB2 could combine mut-p53 and change the DNA binding site of mutant p53, subsequently upregulated the expression of RPRM, BAI-1, and TSAP6 which were the downstream genes of wt-p53, participate in mediating downstream responses to p53, including inhibiting cell proliferation and angiogenesis. The main aim of this study is to investigate the relationship between HspB2 and p53, and provide a novel treatment strategy for pancreatic cancer.

show abstract

Developmental Expression and Functions of the Small Heat Shock Proteins in Drosophila

Cited by 31 publications

References 47 publications

Small heat shock proteins determine synapse number and neuronal activity during development

Small heat shock proteins determine synapse number and neuronal activity during development

Small heat shock proteins determine synapse number and neuronal activity during development

Molecular chaperone HspB2 inhibited pancreatic cancer cell proliferation via activating p53 downstream gene RPRM, BAI1, and TSAP6

Contact Info

Product

Resources

About