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Gene Review

Hspa8  -  heat shock protein 8

Mus musculus

Synonyms: 2410008N15Rik, Heat shock 70 kDa protein 8, Heat shock cognate 71 kDa protein, Hsc70, Hsc71, ...
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Disease relevance of Hspa8


High impact information on Hspa8

  • We identify a chaperone complex composed of (1) the synaptic vesicle cysteine string protein (CSP), thought to function in neurotransmitter release, (2) the ubiquitous heat-shock protein cognate Hsc70, and (3) the SGT protein containing three tandem tetratricopeptide repeats [6].
  • Mechanistic aspects of chaperone cooperation are now emerging from studies on the regulation of certain signal transduction pathways mediated by Hsc70 and Hsp90 in the eukaryotic cytosol [7].
  • In contrast, the distribution of Hsp73 in ScN2a cells was not altered by heat shock; the discrete cytoplasmic structures containing Hsp73 were largely resistant to detergent extraction [8].
  • Of these interacting chaperones, only Hdj-2 and Hsc70 frequently (Hdj-2 > Hsc70) co-localize with both the aggregates in the cellular model and with the NIs in the brains of HD exon 1 transgenic mice [9].
  • Overexpression of Hdj-1 and Hsc70 is also able to protect cell death caused by polyglutamine-expanded tNhtt and their combination proved to be most effective [9].

Chemical compound and disease context of Hspa8


Biological context of Hspa8

  • This study examined the detailed gene expression pattern of three different heat shock proteins (HSPs), Hsc73, Hsj2, and Hsp86, by means of an in situ hybridization method [11].
  • In the present study we show that the chaperoning activity of purified Hsp70 and Hsc70 is minimal under reducing conditions and increases in environments that mimic oxidative stress [12].
  • We suggest that the association with the Hsc70-containing complex prevents the NLS from the access of the import receptor through the C-terminal region of p53(Val-135) at 37 degrees C, whereas its dissociation at 32 degrees C allows rapid nuclear import [13].
  • Regulation of the Dbl proto-oncogene by heat shock cognate protein 70 (Hsc70) [14].
  • We suggested that known ethanol actions on cellular protein trafficking may relate to Hsc70 induction because Hsc70 functions as a molecular chaperone [3].

Anatomical context of Hspa8

  • In situ expression of heat shock proteins, Hsc73, Hsj2 and Hsp86 in the developing tooth germ of mouse lower first molar [11].
  • Immunodepletion of Hsc70 from the reticulocyte lysate caused p53(Val-135) to bind the import receptor [13].
  • Immunostaining reveals the co-localization of the molecular chaperones Hsc70 and Hsp90 with the GFP-myosin in the intermediates, but not in the mature myofibrils [15].
  • Auxilin is an Hsp40 family protein that catalytically supports the uncoating of clathrin-coated vesicles through recruitment of Hsc70 in an ATP hydrolysis-driven process [16].
  • SEB-treated (5 or 100 microg intraperitoneally) mice revealed increased Hsp25 and Hsp72, but not Hsc73, in jejunal lymphocytes and epithelial cells [17].

Associations of Hspa8 with chemical compounds


Physical interactions of Hspa8


Regulatory relationships of Hspa8


Other interactions of Hspa8

  • We show in tumor cells that hypericin targets the heat shock protein (Hsp) 90 chaperone but not Hsp70 (Hsc70) to enhanced ubiquitinylation [24].
  • This study is the first report in which Hsc73, Hsj2, and Hsp86 were distinctly expressed in the developing tooth germ, thus suggesting these HSPs are related to the development and differentiation of odontogenic cells [11].
  • We propose that Hsc70 attenuates Dbl activity by maintaining an inactive conformation in which the amino terminus is "folded over" the catalytic DH-PH domain [14].
  • We examined the effect of heat stress on localization of two sHsps, alphaB-crystallin and Hsp25, and of Hsc70, a member of a different class of heat shock proteins (Hsps), in both undifferentiated and differentiated mouse C2C12 cells [2].
  • These results suggest that these peptide regions must not only be exposed but still in a flexible extended conformation in the mAAT folding intermediates recognized by Hsc70 [22].

Analytical, diagnostic and therapeutic context of Hspa8

  • Structural predictions were confirmed by site-directed mutagenesis of these residues, resulting in loss of binding of BAG1 to Hsc70 in vitro and in cells [25].
  • Here, we report that the C-terminus of Hsc70-interacting protein (CHIP) with a U-box domain is an E3 ubiquitin-ligase collaborating with molecular chaperones Hsp90 and Hsc70 [26].
  • A partial integrin beta 1 subunit-encoding cDNA (Itg beta 1) and a new heat-shock protein 70-like-encoding cDNA (Hsc73) homologous to rat Hsc73 were cloned by differential display and RT-PCR from mouse mammary gland [18].
  • We examined the regulation of the constitutive and stress-induced 70-kD Hsps (Hsc70 and Hsp70, respectively) after sciatic nerve (SN) axotomy in the neonatal mouse [5].
  • Flow cytometry detected a significant 1.2-fold increase in Hsp70/Hsc70 accumulation (P < 0.001) in protoplasts, while Western blotting, quantified by image analysis, showed induction under similar conditions but at lower significance (P < 0.05) [27].


  1. Fusion protein of ATPase domain of Hsc70 with TRP2 acting as a tumor vaccine against B16 melanoma. Zhang, H., Wang, W., Li, Q., Huang, W. Immunol. Lett. (2006) [Pubmed]
  2. Heat stress-induced localization of small heat shock proteins in mouse myoblasts: intranuclear lamin A/C speckles as target for alphaB-crystallin and Hsp25. Adhikari, A.S., Sridhar Rao, K., Rangaraj, N., Parnaik, V.K., Mohan Rao, C.h. Exp. Cell Res. (2004) [Pubmed]
  3. Ethanol-responsive genes in neural cells include the 78-kilodalton glucose-regulated protein (GRP78) and 94-kilodalton glucose-regulated protein (GRP94) molecular chaperones. Miles, M.F., Wilke, N., Elliot, M., Tanner, W., Shah, S. Mol. Pharmacol. (1994) [Pubmed]
  4. Antigenic peptides complexed to phylogenically diverse Hsp70s induce differential immune responses. Kumaraguru, U., Gouffon, C.A., Ivey, R.A., Rouse, B.T., Bruce, B.D. Cell Stress Chaperones (2003) [Pubmed]
  5. Administration of Hsp70 in vivo inhibits motor and sensory neuron degeneration. Tidwell, J.L., Houenou, L.J., Tytell, M. Cell Stress Chaperones (2004) [Pubmed]
  6. A trimeric protein complex functions as a synaptic chaperone machine. Tobaben, S., Thakur, P., Fernández-Chacón, R., Südhof, T.C., Rettig, J., Stahl, B. Neuron (2001) [Pubmed]
  7. Chaperones get in touch: the Hip-Hop connection. Frydman, J., Höhfeld, J. Trends Biochem. Sci. (1997) [Pubmed]
  8. Scrapie prions selectively modify the stress response in neuroblastoma cells. Tatzelt, J., Zuo, J., Voellmy, R., Scott, M., Hartl, U., Prusiner, S.B., Welch, W.J. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  9. Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity. Jana, N.R., Tanaka, M., Wang, G., Nukina, N. Hum. Mol. Genet. (2000) [Pubmed]
  10. Nuclear translocation of heat shock protein 72 in liver cells of halothane-exposed rats. Lin, W.Q., Van Dyke, R.A., Marsh, H.M., Trudell, J.R. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
  11. In situ expression of heat shock proteins, Hsc73, Hsj2 and Hsp86 in the developing tooth germ of mouse lower first molar. Wada, H., Kobayashi, I., Yamaza, H., Matsuo, K., Kiyoshima, T., Akhtar, M., Sakai, T., Koyano, K., Sakai, H. Histochem. J. (2002) [Pubmed]
  12. Differential acquisition of antigenic peptides by Hsp70 and Hsc70 under oxidative conditions. Callahan, M.K., Chaillot, D., Jacquin, C., Clark, P.R., Ménoret, A. J. Biol. Chem. (2002) [Pubmed]
  13. A role for Hsc70 in regulating nucleocytoplasmic transport of a temperature-sensitive p53 (p53Val-135). Akakura, S., Yoshida, M., Yoneda, Y., Horinouchi, S. J. Biol. Chem. (2001) [Pubmed]
  14. Regulation of the Dbl proto-oncogene by heat shock cognate protein 70 (Hsc70). Kauppinen, K.P., Duan, F., Wels, J.I., Manor, D. J. Biol. Chem. (2005) [Pubmed]
  15. Chaperone-mediated folding and assembly of myosin in striated muscle. Srikakulam, R., Winkelmann, D.A. J. Cell. Sci. (2004) [Pubmed]
  16. Structure of the functional fragment of auxilin required for catalytic uncoating of clathrin-coated vesicles. Gruschus, J.M., Han, C.J., Greener, T., Ferretti, J.A., Greene, L.E., Eisenberg, E. Biochemistry (2004) [Pubmed]
  17. Bacterial superantigen-treated intestinal epithelial cells upregulate heat shock proteins 25 and 72 and are resistant to oxidant cytotoxicity. Musch, M.W., Petrof, E.O., Kojima, K., Ren, H., McKay, D.M., Chang, E.B. Infect. Immun. (2004) [Pubmed]
  18. Developmental regulation of murine integrin beta 1 subunit- and Hsc73-encoding genes in mammary gland: sequence of a new mouse Hsc73 cDNA. Soulier, S., Vilotte, J.L., L'Huillier, P.J., Mercier, J.C. Gene (1996) [Pubmed]
  19. Characterization and expression of the mouse Hsc70 gene. Hunt, C.R., Parsian, A.J., Goswami, P.C., Kozak, C.A. Biochim. Biophys. Acta (1999) [Pubmed]
  20. Release of kinesin from vesicles by hsc70 and regulation of fast axonal transport. Tsai, M.Y., Morfini, G., Szebenyi, G., Brady, S.T. Mol. Biol. Cell (2000) [Pubmed]
  21. Effects of dexamethasone, heat shock, and serum responses on the inhibition of Hsc70 synthesis by antisense RNA in NIH 3T3 cells. Li, T., Hightower, L.E. J. Cell. Physiol. (1995) [Pubmed]
  22. Identification of Hsc70 binding sites in mitochondrial aspartate aminotransferase. Artigues, A., Iriarte, A., Martinez-Carrion, M. Arch. Biochem. Biophys. (2006) [Pubmed]
  23. The molecular chaperones Hsp90 and Hsc70 are both necessary and sufficient to activate hormone binding by glucocorticoid receptor. Rajapandi, T., Greene, L.E., Eisenberg, E. J. Biol. Chem. (2000) [Pubmed]
  24. Enhanced ubiquitinylation of heat shock protein 90 as a potential mechanism for mitotic cell death in cancer cells induced with hypericin. Blank, M., Mandel, M., Keisari, Y., Meruelo, D., Lavie, G. Cancer Res. (2003) [Pubmed]
  25. Structural analysis of BAG1 cochaperone and its interactions with Hsc70 heat shock protein. Briknarová, K., Takayama, S., Brive, L., Havert, M.L., Knee, D.A., Velasco, J., Homma, S., Cabezas, E., Stuart, J., Hoyt, D.W., Satterthwait, A.C., Llinás, M., Reed, J.C., Ely, K.R. Nat. Struct. Biol. (2001) [Pubmed]
  26. CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein. Murata, S., Minami, Y., Minami, M., Chiba, T., Tanaka, K. EMBO Rep. (2001) [Pubmed]
  27. A rapid and reliable flow cytometric method for determining Hsp70 levels in tobacco protoplasts. Cronjé, M.J., Snyman, M., Bornman, L., Weir, I.E. Methods in cell science : an official journal of the Society for In Vitro Biology. (2003) [Pubmed]
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