![]() Neurosci Lett 206(1):45–48Īmmirante M, Rosati A, Gentilella A, Festa M, Petrella A, Marzullo L, Pascale M, Belisario MA, Leone A, Turco MC (2008) The activity of hsp90 alpha promoter is regulated by NF-kappa B transcription factors. Nat Commun 5:5484Īmin V, Cumming DV, Latchman DS (1996) Over-expression of heat shock protein 70 protects neuronal cells against both thermal and ischaemic stress but with different efficiencies. Nature 440(7087):1013–1017Īlvira S, Cuellar J, Rohl A, Yamamoto S, Itoh H, Alfonso C, Rivas G, Buchner J, Valpuesta JM (2014) Structural characterization of the substrate transfer mechanism in Hsp70/Hsp90 folding machinery mediated by Hop. J Cell Biol 217(11):3809–3816Īli MM, Roe SM, Vaughan CK, Meyer P, Panaretou B, Piper PW, Prodromou C, Pearl LH (2006) Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nat Commun 10(1):1068Īlford BD, Brandman O (2018) Quantification of Hsp90 availability reveals differential coupling to the heat shock response. Nat Rev Genet 13(10):720–731Īlderson TR, Roche J, Gastall HY, Dias DM, Pritisanac I, Ying J, Bax A, Benesch JLP, Baldwin AJ (2019) Local unfolding of the HSP27 monomer regulates chaperone activity. We review recently described and hallmark mechanistic principles of the HSR, the regulation and functions of HSPs, and contexts in which the HSR is activated and influences cell fate in response to various toxic conditions.Īdelman K, Lis JT (2012) Promoter-proximal pausing of RNA polymerase II: emerging roles in metazoans. Development of effective therapies will, however, require a detailed understanding of the HSR, important features of which continue to be uncovered and are yet to be completely understood. Modulation of the HSR and/or its extended network have, therefore, become attractive treatment strategies for these diseases. The effector molecules of the HSR, the Heat Shock Factors (HSFs) and Heat Shock Proteins (HSPs), are also important regulatory targets in the progression of neurodegenerative diseases and cancers. While named for its vital role in the cellular response to heat stress, various components of the HSR system and the molecular chaperone network execute essential physiological functions as well as responses to other diverse toxic insults. The HSR is, therefore, a critical factor that influences the toxicity of protein stress. ![]() The HSR provides cells with an enhanced ability to endure proteotoxic insults and plays a crucial role in determining subsequent cell death or survival. Cells respond to protein-damaging (proteotoxic) stress by activation of the Heat Shock Response (HSR).
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