a critical chaperone protein that has a high affinity for unfolded polypeptide chains. It binds extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In cooperation with other chaperones, hsp70 stabilizes preexistent proteins against aggregation and mediates the folding of newly translated polypeptides in the cytosol as well as within organelles. Mitochondrial HSP70 is crucial to the import process: mutant forms of HSP70 fail to import precursor proteins. Is anti-apoptotic in sympathetic neurones and mediates this effect primarily by suppressing c-Jun transcriptional signalling. Interacts with tau protein and mediates proper folding of tau. Can promote the degradation of tau protein. Triptolide, a potential therapeutic agent for progression/metastasis of pancreatic cancer, causes pancreatic cancer cell death by induction of apoptosis, an effect mediated by the inhibition of HSP70. Note: This description may include information from UniProtKB.
Protein type: Chaperone; Heat shock protein; Motility/polarity/chemotaxis
Cellular Component: cell-cell adherens junction; centriole; cytoplasm; cytosol; focal adhesion; inclusion body; nucleoplasm; perinuclear region of cytoplasm; ubiquitin ligase complex
Molecular Function: ATP binding; ATPase activity; ATPase activity, coupled; enzyme binding; G-protein-coupled receptor binding; heat shock protein binding; histone deacetylase binding; protein binding; receptor binding; ubiquitin protein ligase binding; unfolded protein binding
Biological Process: activation of NF-kappaB transcription factor; ATP metabolic process; negative regulation of protein ubiquitination; positive regulation of interleukin-8 production; protein refolding; protein stabilization; regulation of mRNA stability; regulation of protein ubiquitination