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Heat shock proteins (HSPs) are a family of proteins produced by cells in response to exposure to stressful conditions. They were first described in relation to heat shock, [1] but are now known to also be expressed during other stresses including exposure to cold, [2] UV light [3] and during wound healing or tissue remodeling. [4]
Heat shock proteins induced by the HSR can help prevent protein aggregation that is associated with common neurodegenerative diseases such as Alzheimer's, Huntington's, or Parkinson's disease. [8] The diagram depicts actions taken when a stress is introduced to the cell. Stress will induce HSF-1 and cause proteins to misfold.
The Heat Shock sequence Element is highly conserved from yeast to humans. [6] Heat shock factor 1 (HSF-1) is the major regulator of heat shock protein transcription in eukaryotes. In the absence of cellular stress, HSF-1 is inhibited by association with heat shock proteins and is therefore not active.
The heat stress response in plants is mediated by heat shock transcription factors and is well conserved across eukaryotes. HSFs are essential in plants’ ability to both sense and respond to stress. [5] The HSFs, which are divided into three families (A, B, and C), encode the expression of heat shock proteins .
By temporarily binding to hydrophobic residues exposed by stress, Hsp70 prevents these partially denatured proteins from aggregating, and inhibits them from refolding. Low ATP is characteristic of heat shock and sustained binding is seen as aggregation suppression, while recovery from heat shock involves substrate binding and nucleotide cycling.
Hsp90 (heat shock protein 90) is a chaperone protein that assists other proteins to fold properly, stabilizes proteins against heat stress, and aids in protein degradation. It also stabilizes a number of proteins required for tumor growth, which is why Hsp90 inhibitors are investigated as anti-cancer drugs.
Molecular chaperones are a diverse family of proteins that function to protect proteins from irreversible aggregation during synthesis and in times of cellular stress.The bacterial molecular chaperone DnaK is an enzyme that couples cycles of ATP binding, hydrolysis, and ADP release by an N-terminal ATP-hydrolyzing domain to cycles of sequestration and release of unfolded proteins by a C ...
Hsp104 is a heat-shock protein.It is known to reverse toxicity of mutant α-synuclein, TDP-43, FUS, and TAF15 in yeast cells. [1] Conserved in prokaryotes (ClpB), fungi, plants and as well as animal mitochondria, there is yet to see hsp104 in multicellular animals.