JNK phosphorylates the HSF1 transcriptional activation domain: Role of JNK in the regulation of the heat shock response

2001 ◽  
Vol 82 (2) ◽  
pp. 326-338 ◽  
Author(s):  
Jeonghyeon Park ◽  
Alice Y.C. Liu
Keyword(s):  
Heat Shock ◽  
Heat Shock Response ◽  
Transcriptional Activation ◽  
Activation Domain ◽  
Transcriptional Activation Domain ◽  
Shock Response

Frazzled/Dcc acts independently of Netrin to promote germline survival during Drosophila oogenesis

Development ◽  
2021 ◽  
Vol 148 (24) ◽  
Author(s):  
Samantha A. Russell ◽  
Kaitlin M. Laws ◽  
Greg J. Bashaw
Keyword(s):  
Cell Death ◽  
Axon Guidance ◽  
Transcriptional Activation ◽  
Nutrient Sensing ◽  
Activation Domain ◽  
Transcriptional Activation Domain ◽  
Egg Chambers ◽  
Death Effector ◽  
Female Germline

ABSTRACT The Netrin receptor Frazzled/Dcc (Fra in Drosophila) functions in diverse tissue contexts to regulate cell migration, axon guidance and cell survival. Fra signals in response to Netrin to regulate the cytoskeleton and also acts independently of Netrin to directly regulate transcription during axon guidance in Drosophila. In other contexts, Dcc acts as a tumor suppressor by directly promoting apoptosis. In this study, we report that Fra is required in the Drosophila female germline for the progression of egg chambers through mid-oogenesis. Loss of Fra in the germline, but not the somatic cells of the ovary, results in the degeneration of egg chambers. Although a failure in nutrient sensing and disruptions in egg chamber polarity can result in degeneration at mid-oogenesis, these factors do not appear to be affected in fra germline mutants. However, similar to the degeneration that occurs in those contexts, the cell death effector Dcp-1 is activated in fra germline mutants. The function of Fra in the female germline is independent of Netrin and requires the transcriptional activation domain of Fra. In contrast to the role of Dcc in promoting cell death, our observations reveal a role for Fra in regulating germline survival by inhibiting apoptosis.

scholarly journals Alpha lipoic acid attenuates ER stress and improves glucose uptake through DNAJB3 cochaperone

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Abdoulaye Diane ◽  
Naela Mahmoud ◽  
Ilham Bensmail ◽  
Namat Khattab ◽  
Hanan A. Abunada ◽  
...  
Keyword(s):  
Heat Shock ◽  
Er Stress ◽  
Glucose Uptake ◽  
Lipoic Acid ◽  
Heat Shock Response ◽  
Transcriptional Activation ◽  
Hepg2 Cells ◽  
Metabolic Stress ◽  
C2c12 Cells ◽  
Shock Response

AbstractPersistent ER stress, mitochondrial dysfunction and failure of the heat shock response (HSR) are fundamental hallmarks of insulin resistance (IR); one of the early core metabolic aberrations that leads to type 2 diabetes (T2D). The antioxidant α-lipoic acid (ALA) has been shown to attenuate metabolic stress and improve insulin sensitivity in part through activation of the heat shock response (HSR). However, these studies have been focused on a subset of heat shock proteins (HSPs). In the current investigation, we assessed whether ALA has an effect on modulating the expression of DNAJB3/HSP40 cochaperone; a potential therapeutic target with a novel role in mitigating metabolic stress and promoting insulin signaling. Treatment of C2C12 cells with 0.3 mM of ALA triggers a significant increase in the expression of DNAJB3 mRNA and protein. A similar increase in DNAJB3 mRNA was also observed in HepG2 cells. We next investigated the significance of such activation on endoplasmic reticulum (ER) stress and glucose uptake. ALA pre-treatment significantly reduced the expression of ER stress markers namely, GRP78, XBP1, sXBP1 and ATF4 in response to tunicamycin. In functional assays, ALA treatment abrogated significantly the tunicamycin-mediated transcriptional activation of ATF6 while it enhanced the insulin-stimulated glucose uptake and Glut4 translocation. Silencing the expression of DNAJB3 but not HSP72 abolished the protective effect of ALA on tunicamycin-induced ER stress, suggesting thus that DNAJB3 is a key mediator of ALA-alleviated tunicamycin-induced ER stress. Furthermore, the effect of ALA on insulin-stimulated glucose uptake is significantly reduced in C2C12 and HepG2 cells transfected with DNAJB3 siRNA. In summary, our results are supportive of an essential role of DNAJB3 as a molecular target through which ALA alleviates ER stress and improves glucose uptake.

scholarly journals An important role of the heat shock response in infected cells for replication of baculoviruses

Virology ◽  
2010 ◽  
Vol 406 (2) ◽  
pp. 336-341 ◽  
Author(s):  
Yulia V. Lyupina ◽  
Svetlana B. Dmitrieva ◽  
Anna V. Timokhova ◽  
Svetlana N. Beljelarskaya ◽  
Olga G. Zatsepina ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Response ◽  
Shock Response ◽  
Infected Cells

scholarly journals Role of BRCA1 in heat shock response

Oncogene ◽  
2003 ◽  
Vol 22 (1) ◽  
pp. 10-27 ◽  
Author(s):  
Yong Xian Ma ◽  
Saijun Fan ◽  
Jingbo Xiong ◽  
Ren-qi Yuan ◽  
Qinghui Meng ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Response ◽  
Shock Response

Anti-Inflammatory Activity of 15-Deoxy-Δ12,14-PGJ2and 2-Cyclopenten-1-one: Role of the Heat Shock Response

2003 ◽  
Vol 64 (1) ◽  
pp. 85-93 ◽  
Author(s):  
Angela Ianaro ◽  
Armando Ialenti ◽  
Pasquale Maffia ◽  
Paola Di Meglio ◽  
Massimo Di Rosa ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Response ◽  
Inflammatory Activity ◽  
Shock Response ◽  
Anti Inflammatory

scholarly journals Role of HSF1 phopshorylation in heat shock response

2013 ◽  
Vol 27 (S1) ◽  
Author(s):  
Marek Andrzej Budzyñski ◽  
Mikael Puustien ◽  
Jenny Joutsen ◽  
Julis Anckar ◽  
Lea Sistonen
Keyword(s):  
Heat Shock ◽  
Heat Shock Response ◽  
Shock Response

Poly(ADP-ribosyl)ation regulates heat shock factor-1 activity and the heat shock response in murine fibroblasts

2006 ◽  
Vol 84 (5) ◽  
pp. 703-712 ◽  
Author(s):  
Silvia Fossati ◽  
Laura Formentini ◽  
Zhao-Qi Wang ◽  
Flavio Moroni ◽  
Alberto Chiarugi
Keyword(s):  
Heat Shock ◽  
Heat Shock Response ◽  
Mammalian Cells ◽  
Molecular Mechanisms ◽  
Heat Shock Factor ◽  
Binding Motif ◽  
Heat Shock Factor 1 ◽  
Shock Response ◽  
Parp 1

Poly(ADP-ribose) polymerase-1 (PARP-1)-dependent poly(ADP-ribose) formation is emerging as a key regulator of transcriptional regulation, even though the targets and underlying molecular mechanisms have not yet been clearly identified. In this study, we gathered information on the role of PARP-1 activity in the heat shock response of mouse fibroblasts. We show that DNA binding of heat shock factor (HSF)-1 was impaired by PARP-1 activity in cellular extracts, and was higher in PARP-1−/− than in PARP-1+/+ cells. No evidence for HSF-1 poly(ADP-ribosyl)ation or PARP-1 interaction was found, but a poly(ADP-ribose) binding motif was identified in the transcription factor amino acid sequence. Consistent with data on HSF-1, the expression of heat-shock protein (HSP)-70 and HSP–27 was facilitated in cells lacking PARP-1. Thermosensitivity, however, was higher in PARP-1−/− than in PARP-1+/+ cells. Accordingly, we report that heat-shocked PARP-1 null fibroblasts showed an increased activation of proapoptotic JNK and decreased transcriptional efficiency of prosurvival NF-κB compared with wild-type counterparts. The data indicate that poly(ADP-ribosyl)ation finely regulates HSF-1 activity, and emphasize the complex role of PARP-1 in the heat-shock response of mammalian cells.

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