The expression patterns of heat shock genes and proteins and their role during vertebrate's development

Rupik, Weronika; Jasik, Krzysztof; Bembenek, Jadwiga; Widłak, Wiesława

doi:10.1016/j.cbpa.2011.04.002

Cited by 76 publications

(52 citation statements)

References 207 publications

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“…However, besides this classical role, in recent years stress-independent and tissue-specific expression and function have been reported for several members of the Hsp gene family (Michaud and Tanguay, 2003;Rupik et al, 2011).…”

Section: Discussionmentioning

confidence: 99%

Drosophila small heat shock protein CryAB ensures structural integrity of developing muscles, and proper muscle and heart performance

et al. 2015

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Molecular chaperones, such as the small heat shock proteins (sHsps), maintain normal cellular function by controlling protein homeostasis in stress conditions. However, sHsps are not only activated in response to environmental insults, but also exert developmental and tissuespecific functions that are much less known. Here, we show that during normal development the Drosophila sHsp CryAB [L(2)efl] is specifically expressed in larval body wall muscles and accumulates at the level of Z-bands and around myonuclei. CryAB features a conserved actin-binding domain and, when attenuated, leads to clustering of myonuclei and an altered pattern of sarcomeric actin and the Z-band-associated actin crosslinker Cheerio (filamin). Our data suggest that CryAB and Cheerio form a complex essential for muscle integrity: CryAB colocalizes with Cheerio and, as revealed by mass spectrometry and co-immunoprecipitation experiments, binds to Cheerio, and the muscle-specific attenuation of cheerio leads to CryAB-like sarcomeric phenotypes. Furthermore, muscle-targeted expression of CryAB R120G , which carries a mutation associated with desmin-related myopathy (DRM), results in an altered sarcomeric actin pattern, in affected myofibrillar integrity and in Z-band breaks, leading to reduced muscle performance and to marked cardiac arrhythmia. Taken together, we demonstrate that CryAB ensures myofibrillar integrity in Drosophila muscles during development and propose that it does so by interacting with the actin crosslinker Cheerio. The evidence that a DRM-causing mutation affects CryAB muscle function and leads to DRM-like phenotypes in the fly reveals a conserved stress-independent role of CryAB in maintaining muscle cell cytoarchitecture.

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Section: Discussionmentioning

confidence: 99%

Drosophila small heat shock protein CryAB ensures structural integrity of developing muscles, and proper muscle and heart performance

et al. 2015

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“…In vertebrates, embryonic development requires the expression of the HSP70 family members, which intervene as modulators in many developmental events (Rupik et al, 2011). In our previous work, we have shown that the inducible ScHSP70a and ScHSP70b mRNAs were maternal original, and their levels were significantly decreased after the blastula stage (Wang et al, 2014).…”

Section: During the Embryonic Developmentmentioning

confidence: 99%

Comparative analysis of sequence feature and expression of two heat shock cognate 70 genes in mandarin fish Siniperca chuatsi

Wang

Zeng

et al. 2015

Gene

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“…HSPH1, HSPA8, HSP90AA1). Expression of some HSPs is developmentally regulated or restricted to specific cells (Rupik et al, 2011;Ji et al, 2012). The HSR is regulated by Heat Shock Factors (HSFs), which are major transcriptional activators of HSP genes.…”

Section: Introductionmentioning

confidence: 97%

Crosstalk between HSF1 and HSF2 during the heat shock response in mouse testes

Korfanty

Stokowy

Widłak

et al. 2014

The International Journal of Biochemistry & Cell Biology

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Heat Shock Factor 1 (HSF1) is the primary transcription factor responsible for the response to cellular stress, while HSF2 becomes activated during development and differentiation, including spermatogenesis. Although both factors are indispensable for proper spermatogenesis, activation of HSF1 by heat shock initiates apoptosis of spermatogenic cells leading to infertility of males. To characterize mechanisms assisting such heat induced apoptosis we studied how HSF1 and HSF2 cooperate during the heat shock response. For this purpose we used chromatin immunoprecipitation and the proximity ligation approaches. We looked for co-occupation of binding sites by HSF1 and HSF2 in untreated (32 °C) or heat shocked (at 38 °C or 43 °C) spermatocytes, which are cells the most sensitive to hyperthermia. At the physiological temperature or after mild hyperthermia at 38 °C, the sharing of binding sites for both HSFs was observed mainly in promoters of Hsp genes and other stress-related genes. Strong hyperthermia at 43 °C resulted in an increased binding of HSF1 and releasing of HSF2, hence co-occupation of promoter regions was not detected any more. The close proximity of HSF1 and HSF2 (and/or existence of HSF1/HSF2 complexes) was frequent at the physiological temperature. Temperature elevation resulted in a decreased number of such complexes and they were barely detected after strong hyperthermia at 43 °C. We have concluded that at the physiological temperature HSF1 and HSF2 cooperate in spermatogenic cells. However, temperature elevation causes remodeling of chromatin binding and interactions between HSFs are disrupted. This potentially affects the regulation of stress response and contributes to the heat sensitivity of these cells.

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The expression patterns of heat shock genes and proteins and their role during vertebrate's development

Cited by 76 publications

References 207 publications

Drosophila small heat shock protein CryAB ensures structural integrity of developing muscles, and proper muscle and heart performance

Drosophila small heat shock protein CryAB ensures structural integrity of developing muscles, and proper muscle and heart performance

Comparative analysis of sequence feature and expression of two heat shock cognate 70 genes in mandarin fish Siniperca chuatsi

Crosstalk between HSF1 and HSF2 during the heat shock response in mouse testes

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