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Gene Review

HSBP1  -  heat shock factor binding protein 1

Homo sapiens

Synonyms: HSF1BP, Heat shock factor-binding protein 1, NPC-A-13, Nasopharyngeal carcinoma-associated antigen 13
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Disease relevance of HSBP1

  • They also identify two new key protagonists in the complex scenario of breast tumor cell invasiveness in vitro, that is, hsbp1 and hsp90, which deserve further and more extensive studies as potential and attractive molecular targets for anti-breast cancer treatments [1].
  • Xeroderma pigmentosum fibroblasts, complementation group A (XP12BE) had 20-25% more ESS at each dose than the BPDE-treated normal (HSBP) cells [2].

High impact information on HSBP1

  • Alteration in the level of HSBP1 expression in C. elegans has severe effects on survival of the animals after thermal and chemical stress, consistent with a role for HSBP1 as a negative regulator of the heat shock response [3].
  • Heat shock factor-binding protein (HSBP) 1 is a small, evolutionarily conserved protein originally identified in a yeast two-hybrid screen using the trimerization domain of heat shock factor (HSF) 1 as the bait [4].
  • We present here the first evidence that the upregulation of some stress-related genes, most noticeably heat shock factor binding protein-1 (hsbp1) and heat shock protein 90 (hsp-90), is involved in the acquisition of an in vitro more invasive phenotype by cells treated with midregion PTHrP [1].
  • Cells treated with 4 microM BPDE and allowed 12 h of incubation to perform excision repair showed removal of 60% of the initial number of ESS from HSBP DNA and 40% of the ESS from XP-A DNA [2].
  • Zea mays contains two HSBP paralogs, EMP2 and HSBP2, which exhibit differential accumulation during the HSR and plant development [5].

Biological context of HSBP1

  • To establish a biological role for HSBP1, the homologous Caenorhabditis elegans protein was overexpressed in body wall muscle cells and was shown to block activation of the heat shock response from a heat shock promoter-reporter construct [3].
  • It is shown that CeReS-18 mediated cell cycle arrest of both human diploid fibroblasts (HSBP) and mouse fibroblasts (Swiss 3T3) results in the maintenance of the RB protein in the hypophosphorylated state, consistent with a late G1 arrest site [6].
  • DNA damage was also induced in HSBP cells following treatment with selenium but only in the presence of reduced glutathione [7].

Anatomical context of HSBP1

  • Cadmium (Cd2+), nickel (Ni2+) and chromate (Cr2O7) reduced the cloning efficiency of HSBP cells more than that of CHO cells whereas the reverse was true after treatment with mercury (Hg2+), manganese (Mn2+) and cobalt (Co2+) [7].
  • However, challenging cultured cells with H. pylori previously incubated with rabbit anti-HSBP IgG resulted in significant inhibition of bacterial adherence [8].

Analytical, diagnostic and therapeutic context of HSBP1

  • Analytical ultracentrifugation and native PAGE studies indicate that HSBP1 is predominantly trimeric over a wide concentration range [4].


  1. PTHrP [67-86] regulates the expression of stress proteins in breast cancer cells inducing modifications in urokinase-plasminogen activator and MMP-1 expression. Luparello, C., Sirchia, R., Pupello, D. J. Cell. Sci. (2003) [Pubmed]
  2. Quantitation of carcinogen-induced DNA damage and repair in human cells with the UVR ABC excision nuclease from Escherichia coli. Van Houten, B., Masker, W.E., Carrier, W.L., Regan, J.D. Carcinogenesis (1986) [Pubmed]
  3. Negative regulation of the heat shock transcriptional response by HSBP1. Satyal, S.H., Chen, D., Fox, S.G., Kramer, J.M., Morimoto, R.I. Genes Dev. (1998) [Pubmed]
  4. Structure-function analysis of the heat shock factor-binding protein reveals a protein composed solely of a highly conserved and dynamic coiled-coil trimerization domain. Tai, L.J., McFall, S.M., Huang, K., Demeler, B., Fox, S.G., Brubaker, K., Radhakrishnan, I., Morimoto, R.I. J. Biol. Chem. (2002) [Pubmed]
  5. The maize heat shock factor-binding protein paralogs EMP2 and HSBP2 interact non-redundantly with specific heat shock factors. Fu, S., Rogowsky, P., Nover, L., Scanlon, M.J. Planta (2006) [Pubmed]
  6. Role of the retinoblastoma protein in cell cycle arrest mediated by a novel cell surface proliferation inhibitor. Enebo, D.J., Fattaey, H.K., Moos, P.J., Johnson, T.C. J. Cell. Biochem. (1994) [Pubmed]
  7. Metal-induced DNA damage and repair in human diploid fibroblasts and Chinese hamster ovary cells. Hamilton-Koch, W., Snyder, R.D., Lavelle, J.M. Chem. Biol. Interact. (1986) [Pubmed]
  8. Involvement of the heparan sulphate-binding proteins of Helicobacter pylori in its adherence to HeLa S3 and Kato III cell lines. Guzman-Murillo, M.A., Ruiz-Bustos, E., Ho, B., Ascencio, F. J. Med. Microbiol. (2001) [Pubmed]
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