BAG1

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BCL2-associated athanogene
Protein BAG1 PDB 1hx1.png
PDB rendering based on 1hx1.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols BAG1 ; BAG-1; HAP; RAP46
External IDs OMIM601497 MGI108047 HomoloGene3190 GeneCards: BAG1 Gene
RNA expression pattern
PBB GE BAG1 211475 s at tn.png
PBB GE BAG1 202387 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 573 12017
Ensembl ENSG00000107262 ENSMUSG00000028416
UniProt Q99933 Q60739
RefSeq (mRNA) NM_001172415 NM_001171739
RefSeq (protein) NP_001165886 NP_001165210
Location (UCSC) Chr 9:
33.25 – 33.26 Mb
Chr 4:
40.94 – 40.95 Mb
PubMed search [1] [2]

BAG family molecular chaperone regulator 1 is a protein that in humans is encoded by the BAG1 gene.[1]

Function[edit]

The oncogene BCL2 is a membrane protein that blocks a step in a pathway leading to apoptosis or programmed cell death. The protein encoded by this gene binds to BCL2 and is referred to as BCL2-associated athanogene. It enhances the anti-apoptotic effects of BCL2 and represents a link between growth factor receptors and anti-apoptotic mechanisms. At least three protein isoforms are encoded by this mRNA through the use of alternative translation initiation sites, including a non-AUG site.[2]

Clinical significance[edit]

BAG gene has been implicated in age related neurodegenerative diseases as Alzheimer's. It has been demonstrated that BAG1 and BAG 3 regulate the proteasomal and lysosomal protein elimination pathways, respectively.[3]

Interactions[edit]

BAG1 has been shown to interact with:

References[edit]

  1. ^ Takayama S, Sato T, Krajewski S, Kochel K, Irie S, Millan JA, Reed JC (March 1995). "Cloning and functional analysis of BAG-1: a novel Bcl-2-binding protein with anti-cell death activity". Cell 80 (2): 279–84. doi:10.1016/0092-8674(95)90410-7. PMID 7834747. 
  2. ^ "Entrez Gene: BAG1 BCL2-associated athanogene". 
  3. ^ Gamerdinger M, Hajieva P, Kaya AM, Wolfrum U, Hartl FU, Behl C (2009). "Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3". EMBO J. 28 (7): 889–901. doi:10.1038/emboj.2009.29. PMC 2647772. PMID 19229298. Lay summaryPhysorg. 
  4. ^ Shatkina L, Mink S, Rogatsch H, Klocker H, Langer G, Nestl A, Cato AC (October 2003). "The cochaperone Bag-1L enhances androgen receptor action via interaction with the NH2-terminal region of the receptor". Mol. Cell. Biol. 23 (20): 7189–97. doi:10.1128/mcb.23.20.7189-7197.2003. PMC 230325. PMID 14517289. 
  5. ^ Knee DA, Froesch BA, Nuber U, Takayama S, Reed JC (April 2001). "Structure-function analysis of Bag1 proteins. Effects on androgen receptor transcriptional activity". J. Biol. Chem. 276 (16): 12718–24. doi:10.1074/jbc.M010841200. PMID 11278763. 
  6. ^ Froesch BA, Takayama S, Reed JC (May 1998). "BAG-1L protein enhances androgen receptor function". J. Biol. Chem. 273 (19): 11660–6. doi:10.1074/jbc.273.19.11660. PMID 9565586. 
  7. ^ Wang HG, Takayama S, Rapp UR, Reed JC (July 1996). "Bcl-2 interacting protein, BAG-1, binds to and activates the kinase Raf-1". Proc. Natl. Acad. Sci. U.S.A. 93 (14): 7063–8. doi:10.1073/pnas.93.14.7063. PMC 38936. PMID 8692945. 
  8. ^ Guzey M, Takayama S, Reed JC (Dec 2000). "BAG1L enhances trans-activation function of the vitamin D receptor". J. Biol. Chem. 275 (52): 40749–56. doi:10.1074/jbc.M004977200. PMID 10967105. 
  9. ^ Kullmann M, Schneikert J, Moll J, Heck S, Zeiner M, Gehring U, Cato AC (June 1998). "RAP46 is a negative regulator of glucocorticoid receptor action and hormone-induced apoptosis". J. Biol. Chem. 273 (23): 14620–5. doi:10.1074/jbc.273.23.14620. PMID 9603979. 
  10. ^ Schneikert J, Hübner S, Langer G, Petri T, Jäättelä M, Reed J, Cato AC (Dec 2000). "Hsp70-RAP46 interaction in downregulation of DNA binding by glucocorticoid receptor". EMBO J. 19 (23): 6508–16. doi:10.1093/emboj/19.23.6508. PMC 305849. PMID 11101523. 
  11. ^ Takayama S, Bimston DN, Matsuzawa S, Freeman BC, Aime-Sempe C, Xie Z, Morimoto RI, Reed JC (August 1997). "BAG-1 modulates the chaperone activity of Hsp70/Hsc70". EMBO J. 16 (16): 4887–96. doi:10.1093/emboj/16.16.4887. PMC 1170124. PMID 9305631. 
  12. ^ Takayama S, Xie Z, Reed JC (January 1999). "An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators". J. Biol. Chem. 274 (2): 781–6. doi:10.1074/jbc.274.2.781. PMID 9873016. 
  13. ^ Lin J, Hutchinson L, Gaston SM, Raab G, Freeman MR (August 2001). "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". J. Biol. Chem. 276 (32): 30127–32. doi:10.1074/jbc.M010237200. PMID 11340068. 
  14. ^ Hung WJ, Roberson RS, Taft J, Wu DY (May 2003). "Human BAG-1 proteins bind to the cellular stress response protein GADD34 and interfere with GADD34 functions". Mol. Cell. Biol. 23 (10): 3477–86. doi:10.1128/mcb.23.10.3477-3486.2003. PMC 164759. PMID 12724406. 
  15. ^ Liu R, Takayama S, Zheng Y, Froesch B, Chen GQ, Zhang X, Reed JC, Zhang XK (July 1998). "Interaction of BAG-1 with retinoic acid receptor and its inhibition of retinoic acid-induced apoptosis in cancer cells". J. Biol. Chem. 273 (27): 16985–92. doi:10.1074/jbc.273.27.16985. PMID 9642262. 
  16. ^ Matsuzawa S, Takayama S, Froesch BA, Zapata JM, Reed JC (May 1998). "p53-inducible human homologue of Drosophila seven in absentia (Siah) inhibits cell growth: suppression by BAG-1". EMBO J. 17 (10): 2736–47. doi:10.1093/emboj/17.10.2736. PMC 1170614. PMID 9582267. 

Further reading[edit]