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Gene Review

BAG1  -  BCL2-associated athanogene

Homo sapiens

Synonyms: BAG family molecular chaperone regulator 1, BAG-1, Bcl-2-associated athanogene 1, HAP, RAP46
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Disease relevance of BAG1


Psychiatry related information on BAG1

  • Additionally, these studies suggest that regulation of GR-mediated plasticity may play a role in the treatment of bipolar disorder and raise the possibility that agents affecting BAG-1 more directly may represent novel therapies for this devastating illness [5].

High impact information on BAG1

  • Bag (Bcl2-associated athanogene) domains occur in a class of cofactors of the eukaryotic chaperone 70-kilodalton heat shock protein (Hsp70) family [6].
  • Here we show that Bag1, a co-chaperone for heat-shock protein 70 (Hsp70), coordinates signals for cell growth in response to cell stress, by downregulating the activity of Raf-1 kinase [7].
  • BAG-1, a shorter isoform with only a duplication of the [EEX(4)] sequence, does not inhibit GR activity [8].
  • We suggest that Siah-1A may be an important mediator of p53-dependent cell-cycle arrest and demonstrate that Siah-1A is directly inhibited by BAG-1 [9].
  • p53-inducible human homologue of Drosophila seven in absentia (Siah) inhibits cell growth: suppression by BAG-1 [9].

Chemical compound and disease context of BAG1


Biological context of BAG1


Anatomical context of BAG1


Associations of BAG1 with chemical compounds


Physical interactions of BAG1


Regulatory relationships of BAG1

  • Thus, BAG-1 regulates the Hsc70 ATPase in a manner contrary to the Hsc70-interacting protein Hip, which stabilizes the ADP-bound state [22].
  • This effect was titratable, and higher levels of wild-type but not a mutant form of Bag1 further inhibited Hsp70 refolding by up to a factor of 5 [23].
  • In addition, because effects of BAG-1 on regulated secretion of soluble HB-EGF were also identified, this interaction has the potential to alter the signaling capabilities of both the membrane-anchored and the diffusible forms of the growth factor [18].
  • Over-expression of BAG-1 significantly inhibited p53-induced growth arrest in 293 cells without preventing p53 transactivation of reporter gene plasmids [9].
  • Here we show that BAG-1 is highly expressed in gastrointestinal epithelial cells and accumulates at the Golgi apparatus, probably through interaction with COPI coated structure [16].

Other interactions of BAG1

  • Here we show that BAG-1 is a regulator of the Hsc70 chaperone [22].
  • We reported previously the cloning of a bradyzoite-specific gene BAG1/hsp30 (previously referred to as BAG5) encoding a cytoplasmic antigen related to small heat shock proteins [15].
  • Both BAG-1 and BAG-3/CAIR-1 interact with Bcl-2 and have been shown to have a supra-additive anti-apoptotic effect with Bcl-2 [24].
  • Bag1 functions in vivo as a negative regulator of Hsp70 chaperone activity [23].
  • BAG-1 expression in hyperplastic and neoplastic prostate tissue: is there any relationship with BCL-related proteins and androgen receptor status [4]?

Analytical, diagnostic and therapeutic context of BAG1


  1. Expression and location of Hsp70/Hsc-binding anti-apoptotic protein BAG-1 and its variants in normal tissues and tumor cell lines. Takayama, S., Krajewski, S., Krajewska, M., Kitada, S., Zapata, J.M., Kochel, K., Knee, D., Scudiero, D., Tudor, G., Miller, G.J., Miyashita, T., Yamada, M., Reed, J.C. Cancer Res. (1998) [Pubmed]
  2. BAG-1 proteins protect cardiac myocytes from simulated ischemia/reperfusion-induced apoptosis via an alternate mechanism of cell survival independent of the proteasome. Townsend, P.A., Cutress, R.I., Carroll, C.J., Lawrence, K.M., Scarabelli, T.M., Packham, G., Stephanou, A., Latchman, D.S. J. Biol. Chem. (2004) [Pubmed]
  3. BAG-1 expression in normal and neoplastic endometrium. Moriyama, T., Littell, R.D., Debernardo, R., Oliva, E., Lynch, M.P., Rueda, B.R., Duska, L.R. Gynecol. Oncol. (2004) [Pubmed]
  4. BAG-1 expression in hyperplastic and neoplastic prostate tissue: is there any relationship with BCL-related proteins and androgen receptor status? Bozdogan, O., Atasoy, P., Bozdogan, N., Erekul, S., Batislam, E., Yilmaz, E., Başar, M.M. Tumori. (2005) [Pubmed]
  5. The anti-apoptotic, glucocorticoid receptor cochaperone protein BAG-1 is a long-term target for the actions of mood stabilizers. Zhou, R., Gray, N.A., Yuan, P., Li, X., Chen, J., Chen, G., Damschroder-Williams, P., Du, J., Zhang, L., Manji, H.K. J. Neurosci. (2005) [Pubmed]
  6. Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors. Sondermann, H., Scheufler, C., Schneider, C., Hohfeld, J., Hartl, F.U., Moarefi, I. Science (2001) [Pubmed]
  7. Bag1-Hsp70 mediates a physiological stress signalling pathway that regulates Raf-1/ERK and cell growth. Song, J., Takeda, M., Morimoto, R.I. Nat. Cell Biol. (2001) [Pubmed]
  8. A nuclear action of the eukaryotic cochaperone RAP46 in downregulation of glucocorticoid receptor activity. Schneikert, J., Hübner, S., Martin, E., Cato, A.C. J. Cell Biol. (1999) [Pubmed]
  9. p53-inducible human homologue of Drosophila seven in absentia (Siah) inhibits cell growth: suppression by BAG-1. Matsuzawa, S., Takayama, S., Froesch, B.A., Zapata, J.M., Reed, J.C. EMBO J. (1998) [Pubmed]
  10. BAG-1 accelerates cell motility of human gastric cancer cells. Naishiro, Y., Adachi, M., Okuda, H., Yawata, A., Mitaka, T., Takayama, S., Reed, J.C., Hinoda, Y., Imai, K. Oncogene (1999) [Pubmed]
  11. Interaction of BAG1 and Hsp70 mediates neuroprotectivity and increases chaperone activity. Liman, J., Ganesan, S., Dohm, C.P., Krajewski, S., Reed, J.C., Bähr, M., Wouters, F.S., Kermer, P. Mol. Cell. Biol. (2005) [Pubmed]
  12. BAG1L enhances trans-activation function of the vitamin D receptor. Guzey, M., Takayama, S., Reed, J.C. J. Biol. Chem. (2000) [Pubmed]
  13. Cloning of cDNAs encoding the human BAG1 protein and localization of the human BAG1 gene to chromosome 9p12. Takayama, S., Kochel, K., Irie, S., Inazawa, J., Abe, T., Sato, T., Druck, T., Huebner, K., Reed, J.C. Genomics (1996) [Pubmed]
  14. BAG-1 modulates the chaperone activity of Hsp70/Hsc70. Takayama, S., Bimston, D.N., Matsuzawa, S., Freeman, B.C., Aime-Sempe, C., Xie, Z., Morimoto, R.I., Reed, J.C. EMBO J. (1997) [Pubmed]
  15. Disruption of the Toxoplasma gondii bradyzoite-specific gene BAG1 decreases in vivo cyst formation. Zhang, Y.W., Kim, K., Ma, Y.F., Wittner, M., Tanowitz, H.B., Weiss, L.M. Mol. Microbiol. (1999) [Pubmed]
  16. Accumulation of Hsp70/Hsc70 molecular chaperone regulator BAG-1 on COPI-coated structures in gastric epithelial cells. Takamura, A., Adachi, M., Wada, I., Mitaka, T., Takayama, S., Imai, K. Int. J. Oncol. (2003) [Pubmed]
  17. HGF receptor associates with the anti-apoptotic protein BAG-1 and prevents cell death. Bardelli, A., Longati, P., Albero, D., Goruppi, S., Schneider, C., Ponzetto, C., Comoglio, P.M. EMBO J. (1996) [Pubmed]
  18. BAG-1 is a novel cytoplasmic binding partner of the membrane form of heparin-binding EGF-like growth factor: a unique role for proHB-EGF in cell survival regulation. Lin, J., Hutchinson, L., Gaston, S.M., Raab, G., Freeman, M.R. J. Biol. Chem. (2001) [Pubmed]
  19. The carboxyl-terminal lobe of Hsc70 ATPase domain is sufficient for binding to BAG1. Brive, L., Takayama, S., Briknarová, K., Homma, S., Ishida, S.K., Reed, J.C., Ely, K.R. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  20. Polypyrimidine tract binding protein and poly r(C) binding protein 1 interact with the BAG-1 IRES and stimulate its activity in vitro and in vivo. Pickering, B.M., Mitchell, S.A., Evans, J.R., Willis, A.E. Nucleic Acids Res. (2003) [Pubmed]
  21. Interaction of BAG-1 with retinoic acid receptor and its inhibition of retinoic acid-induced apoptosis in cancer cells. Liu, R., Takayama, S., Zheng, Y., Froesch, B., Chen, G.Q., Zhang, X., Reed, J.C., Zhang, X.K. J. Biol. Chem. (1998) [Pubmed]
  22. GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1. Höhfeld, J., Jentsch, S. EMBO J. (1997) [Pubmed]
  23. Bag1 functions in vivo as a negative regulator of Hsp70 chaperone activity. Nollen, E.A., Brunsting, J.F., Song, J., Kampinga, H.H., Morimoto, R.I. Mol. Cell. Biol. (2000) [Pubmed]
  24. What's in the 'BAG'?--A functional domain analysis of the BAG-family proteins. Doong, H., Vrailas, A., Kohn, E.C. Cancer Lett. (2002) [Pubmed]
  25. Cloning and characterization of the human BAG-1 gene promoter: upregulation by tumor-derived p53 mutants. Yang, X., Pater, A., Tang, S.C. Oncogene (1999) [Pubmed]
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