Regular ArticleImportance of the ATP-Binding Domain and Nucleolar Localization Domain of HSP72 in the Protection of Nuclear Proteins against Heat-Induced Aggregation
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Functional diversity between HSP70 paralogs caused by variable interactions with specific co-chaperones
2020, Journal of Biological ChemistryCitation Excerpt :From the Hsp70 family, only few members have been tested, mainly HSPA1A (stress-inducible Hsp70) and HSPA8 (constitutive Hsp70, HSC70), but mostly not in a comparative way. In particular, HSPA1A up-regulation has been reported as highly effective in withstanding global protein aggregation induced by unfolding events such as heat shock (21) or aggregation of specific thermosensitive proteins such as luciferase (22). However, neither HSPA1A nor HSPA8 up-regulation is very effective in preventing aggregation of disease-associated amyloidogenic proteins in cells, although results may vary depending on the system or the type of the substrate (18, 19).
Geranylgeranylacetone protects rat and striatum neurons against heat injury via induction of Hsp70
2009, Environmental Toxicology and PharmacologyHuman Fas-associated factor 1 interacts with heat shock protein 70 and negatively regulates chaperone activity
2005, Journal of Biological ChemistryCitation Excerpt :It seems that the chaperone activity of Hsp70, based on ATP hydrolysis as energy source, does not affect SAPK/JNK activity. However, the relative roles of ABD and chaperone function of Hsp70 are not clear (33). In this study, the ABD deletion mutant of Hsp70 showed elevated chaperone activity, although lower than that of the full form of Hsp70, suggesting that ABD, having a smaller domain (amino acids 120–428) in this study than the conventional ABD-(1–428), is not indispensable for the chaperone activity.
Heat shock protein 72 binds and protects dihydrofolate reductase against oxidative injury
2004, Biochemical and Biophysical Research CommunicationsCitation Excerpt :At least two hypotheses may explain this finding: (1) MTX causes an allosteric change in DHFR, disabling its association with Hsp72, or (2) MTX and Hsp72 share a common binding site on DHFR, but MTX by way of a higher affinity is able to preferentially bind to DHFR and displace Hsp72. The dependence of the interaction on nucleotides brings further insights into the association of Hsp72 with DHFR in that it is consistent with previous data that show ATP affects substrate release by chaperones [25,26]. In the absence or low concentrations of ATP, Hsp72–DHFR binding is enhanced.
Nuclear staining for the small heat shock protein αB-crystallin colocalizes with splicing factor SC35
2003, European Journal of Cell Biology