Cell
MinireviewProtein traffic on the heat shock promoter: Parking, stalling, and trucking along
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Cited by (351)
Salinity and bisphenol A alter cellular homeostasis and immune defense by heat shock proteins in the intertidal crab Macrophthalmus japonicus
2019, Estuarine, Coastal and Shelf ScienceCitation Excerpt :In addition, HSPs play important roles in both innate and adaptive immune activation and responses (Srivastava, 2002; Roberts et al., 2010). HSP70, widely used as a biomarker, is involved in various cellular mechanisms, including the biosynthesis and translocation of proteins, degradation of denatured proteins, cell cycle progression, and apoptosis (Lis and Wu, 1993). HSP70 induction and subsequent quantification has been used as a sensitive tool for aquatic toxicity risk assessment (Liu et al., 2012).
Celastrol, an oral heat shock activator, ameliorates multiple animal disease models of cell death
2015, Cell Stress and ChaperonesRNAi screen in Drosophila larvae identifies histone deacetylase 3 as a positive regulator of the hsp70 heat shock gene expression during heat shock
2014, Biochimica et Biophysica Acta - Gene Regulatory MechanismsCitation Excerpt :Under normal conditions, hsp70 is transcribed at low levels but within seconds undergoes a several hundred-fold increase in transcription in response to heat shock [5]. This rapid activation is brought about by the activities of a number of factors, including the heat shock factor, HSF, and the Pol II kinase, P-TEFb [6,7]. The rapid induction of the heat shock genes and the ability to visualize the binding and behavior of transcription factors at the heat shock loci in vivo make it an ideal model gene to study transcription mechanisms [8].
Transcriptional regulation of small HSP - HSF1 and beyond
2012, International Journal of Biochemistry and Cell BiologyCitation Excerpt :HSF1, 2, and 4 are also essential for embryonic development (reviewed in Abane and Mezger, 2010) and we will see that they participate to the developmental, stress-induced, and disease-related expression of sHsp. Interestingly, in Drosophila, all hsp promoters contain GA dinucleotide repeats (i.e. (GA or CT)nn; Gilmour et al., 1989) that bind a GAGA factor protein, which keep the hsp promoters “preset” in an active chromatin configuration (Lis and Wu, 1993; Wallrath et al., 1994), ready for the transcriptional activation following a stress. These GAGA factors permit the efficient pausing of the RNA polymerase, which is transcriptionally engaged on the hsp70 and hsp26 promoter (Core and Lis, 2008; Gilmour, 2009; Price, 2008; Rasmussen and Lis, 1993).
Evolution goes GAGA: GAGA binding proteins across kingdoms
2012, Biochimica et Biophysica Acta - Gene Regulatory Mechanisms