Biology:BAG4

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

BAG family molecular chaperone regulator 4 is a protein that in humans is encoded by the BAG4 gene.[1][2][3]

Function

The protein encoded by this gene is a member of the BAG1-related protein family. BAG1 is an anti-apoptotic protein that functions through interactions with a variety of cell apoptosis and growth related proteins including BCL-2, Raf-protein kinase, steroid hormone receptors, growth factor receptors and members of the heat shock protein 70 kDa family. This protein contains a BAG domain near the C-terminus, which could bind and inhibit the chaperone activity of Hsc70/Hsp70. This protein was found to be associated with the death domain of tumor necrosis factor receptor type 1 (TNF-R1) and death receptor-3 (DR3), and thereby negatively regulates downstream cell death signaling. The regulatory role of this protein in cell death was demonstrated in epithelial cells which undergo apoptosis while integrin mediated matrix contacts are lost.[3]

Interactions

BAG4 has been shown to interact with:

References

  1. "An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators". J Biol Chem 274 (2): 781–6. Feb 1999. doi:10.1074/jbc.274.2.781. PMID 9873016. 
  2. 2.0 2.1 "Prevention of constitutive TNF receptor 1 signaling by silencer of death domains". Science 283 (5401): 543–6. Feb 1999. doi:10.1126/science.283.5401.543. PMID 9915703. Bibcode1999Sci...283..543J. 
  3. 3.0 3.1 "Entrez Gene: BAG4 BCL2-associated athanogene 4". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9530. 
  4. "Involvement of a chaperone regulator, Bcl2-associated athanogene-4, in apolipoprotein B mRNA editing". J. Biol. Chem. 278 (52): 52988–96. Dec 2003. doi:10.1074/jbc.M310153200. PMID 14559896. 
  5. 5.0 5.1 "Tumor necrosis factor receptor 1 is an ATPase regulated by silencer of death domain". Mol. Cell. Biol. 22 (8): 2536–43. Apr 2002. doi:10.1128/MCB.22.8.2536-2543.2002. PMID 11909948. 

External links

Further reading