Summary

Name HSPA8
Full Name Heat shock cognate 71 kDa protein
Synonyms Heat shock 70 kDa protein 8, Lipopolysaccharide-associated protein 1, LAP-1, LPS-associated protein 1 | HSC70, HSP73, HSPA10
Primary ID P11142
Links - -
Type protein
Relations 13
Function Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488, PubMed:12526792). The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488, PubMed:12526792). The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types

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Relations

Regulator Mechanism target score
+ up-regulates activity img/direct-activation.png binding HSPA8 0.522
Publications: 1 Organism: Homo Sapiens
+ up-regulates activity img/direct-activation.png binding HSPA8 0.892
Publications: 1 Organism: In Vitro
+ up-regulates activity img/direct-activation.png binding HSPA8 0.78
Publications: 1 Organism: In Vitro
+ down-regulates quantity by destabilization img/direct_inhibition.png polyubiquitination HSPA8 0.731
Publications: 1 Organism: Chlorocebus Aethiops
+ up-regulates activity img/direct-activation.png binding RNF5 0.392
Publications: 1 Organism: Homo Sapiens
+ down-regulates quantity by destabilization img/direct_inhibition.png binding HSPA8 0.892
Publications: 1 Organism: Chlorocebus Aethiops
+ up-regulates activity img/indirect-activation.png Chaperone-mediated autophagy 0.7
Publications: 1 Organism: In Vitro
+ down-regulates quantity by destabilization img/direct_inhibition.png binding AP-2/clathrin vescicle 0.526
Publications: 1
+ up-regulates quantity by expression img/indirect-activation.png transcriptional regulation HSPA8 0.2
Publications: 1 Organism: Mus Musculus
+ down-regulates activity img/direct_inhibition.png binding HSPA8 0.639
Publications: 1 Organism: Homo Sapiens
+ form complex img/form-complex.png binding PRP19-CDC5L 0.607
Publications: 1 Organism: Homo Sapiens
+ down-regulates quantity img/direct_inhibition.png binding CFTR 0.659
Publications: 1 Organism: Homo Sapiens
+ up-regulates activity img/direct-activation.png relocalization HSPA8 0.881
Publications: 1