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HSPBP1  -  HSPA (heat shock 70kDa) binding protein,...

Homo sapiens

Synonyms: FES1, HSPBP, Heat shock protein-binding protein 1, Hsp70-binding protein 1, Hsp70-binding protein 2, ...
 
 
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Disease relevance of HSPBP1

  • We report here that HspBP1 antibodies are present in human serum and the levels are elevated approximately twofold in HIV infected patients [1].
  • Heat stress resulted in an increase in Hsp70 levels but no change in HspBP1 levels [2].
 

High impact information on HSPBP1

 

Biological context of HSPBP1

 

Anatomical context of HSPBP1

  • Northern blots of RNA from human tissues indicate that HspBP1 mRNA has a size of approximately 1.7 kilobase pairs and is present in all tissues analyzed but is most abundant in heart and skeletal muscle [8].
  • Truncation mutants of HspBP1 were tested for their ability to inhibit the renaturation of luciferase and bind to Hsp70 in reticulocyte lysate [9].
  • In this study, we provide first time evidence for the stimulating effect of the Hsp70-interacting protein Hip on the chaperone activity in the mammalian cytosol [11].
 

Associations of HSPBP1 with chemical compounds

 

Physical interactions of HSPBP1

  • HspBP1 prevented ATP binding to Hsp70, and therefore this is the likely mechanism of inhibition [8].
  • HspBP1 attenuates the ubiquitin ligase activity of CHIP when complexed with Hsc70 [7].
 

Regulatory relationships of HSPBP1

 

Other interactions of HSPBP1

 

Analytical, diagnostic and therapeutic context of HSPBP1

References

  1. Development of a sensitive assay for the measurement of antibodies against heat shock protein binding protein 1 (HspBP1): increased levels of anti-HspBP1 IgG are prevalent in HIV infected subjects. Papp, D., Prohászka, Z., Kocsis, J., Füst, G., Bánhegyi, D., Raynes, D.A., Guerriero, V. J. Med. Virol. (2005) [Pubmed]
  2. Expression of the cochaperone HspBP1 is not coordinately regulated with Hsp70 expression. Gottwald, E., Herschbach, M., Lahni, B., Miesfeld, R.L., Kunz, S., Raynes, D.A., Guerriero, V. Cell Biol. Int. (2006) [Pubmed]
  3. Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange. Shomura, Y., Dragovic, Z., Chang, H.C., Tzvetkov, N., Young, J.C., Brodsky, J.L., Guerriero, V., Hartl, F.U., Bracher, A. Mol. Cell (2005) [Pubmed]
  4. Mutational analysis of the hsp70-interacting protein Hip. Prapapanich, V., Chen, S., Toran, E.J., Rimerman, R.A., Smith, D.F. Mol. Cell. Biol. (1996) [Pubmed]
  5. The co-chaperone carboxyl terminus of Hsp70-interacting protein (CHIP) mediates alpha-synuclein degradation decisions between proteasomal and lysosomal pathways. Shin, Y., Klucken, J., Patterson, C., Hyman, B.T., McLean, P.J. J. Biol. Chem. (2005) [Pubmed]
  6. BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP. Arndt, V., Daniel, C., Nastainczyk, W., Alberti, S., Höhfeld, J. Mol. Biol. Cell (2005) [Pubmed]
  7. The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator. Alberti, S., Böhse, K., Arndt, V., Schmitz, A., Höhfeld, J. Mol. Biol. Cell (2004) [Pubmed]
  8. Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding protein. Raynes, D.A., Guerriero, V. J. Biol. Chem. (1998) [Pubmed]
  9. HspBP1, an Hsp70 cochaperone, has two structural domains and is capable of altering the conformation of the Hsp70 ATPase domain. McLellan, C.A., Raynes, D.A., Guerriero, V. J. Biol. Chem. (2003) [Pubmed]
  10. HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factor. Kabani, M., McLellan, C., Raynes, D.A., Guerriero, V., Brodsky, J.L. FEBS Lett. (2002) [Pubmed]
  11. Modulation of in vivo HSP70 chaperone activity by Hip and Bag-1. Nollen, E.A., Kabakov, A.E., Brunsting, J.F., Kanon, B., Höhfeld, J., Kampinga, H.H. J. Biol. Chem. (2001) [Pubmed]
  12. Cell surface-bound heat shock protein 70 (Hsp70) mediates perforin-independent apoptosis by specific binding and uptake of granzyme B. Gross, C., Koelch, W., DeMaio, A., Arispe, N., Multhoff, G. J. Biol. Chem. (2003) [Pubmed]
  13. Orthologs in Arabidopsis thaliana of the Hsp70 interacting protein Hip. Webb, M.A., Cavaletto, J.M., Klanrit, P., Thompson, G.A. Cell Stress Chaperones (2001) [Pubmed]
  14. An androgen receptor NH2-terminal conserved motif interacts with the COOH terminus of the Hsp70-interacting protein (CHIP). He, B., Bai, S., Hnat, A.T., Kalman, R.I., Minges, J.T., Patterson, C., Wilson, E.M. J. Biol. Chem. (2004) [Pubmed]
  15. Hsc/Hsp70 interacting protein (hip) associates with CXCR2 and regulates the receptor signaling and trafficking. Fan, G.H., Yang, W., Sai, J., Richmond, A. J. Biol. Chem. (2002) [Pubmed]
  16. Identification of VCP/p97, carboxyl terminus of Hsp70-interacting protein (CHIP), and amphiphysin II interaction partners using membrane-based human proteome arrays. Grelle, G., Kostka, S., Otto, A., Kersten, B., Genser, K.F., Müller, E.C., Wälter, S., Böddrich, A., Stelzl, U., Hänig, C., Volkmer-Engert, R., Landgraf, C., Alberti, S., Höhfeld, J., Strödicke, M., Wanker, E.E. Mol. Cell Proteomics (2006) [Pubmed]
  17. Molecular cloning of human p48, a transient component of progesterone receptor complexes and an Hsp70-binding protein. Prapapanich, V., Chen, S., Nair, S.C., Rimerman, R.A., Smith, D.F. Mol. Endocrinol. (1996) [Pubmed]
  18. Human serum contains detectable levels of the Hsp70 cochaperone HspBP1 and antibodies bound to HspBP1. Raynes, D.A., Thomson, C.A., Stroster, J., Newton, T., Cuneo, P., Guerriero, V. Journal of immunoassay & immunochemistry. (2006) [Pubmed]
 
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