BAG4
BAG4 (BAG cochaperone 4, also known as SODD) is a cytoplasmic member of the BAG family of cochaperones. It inhibits HSP70/HSC70 chaperone activity by promoting substrate release and restrains death receptor signalling. Browse Assay Genie's current range of BAG4 research reagents below, or read on for the biology behind the target.
BAG4 inhibits the chaperone activity of HSP70 and HSC70 by promoting substrate release. It also prevents constitutive signalling by TNFRSF1A (TNF-R1), and acts as a negative regulator of PRKN translocation to damaged mitochondria. The protein contains a BAG domain near the C-terminus, which can bind Hsc70/Hsp70 and inhibit their chaperone activity.
The human BAG4 gene encodes a member of the BAG1-related protein family. BAG1 is an anti-apoptotic protein that acts through interactions with a variety of 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. BAG4 belongs to the HGNC gene group of BAG cochaperones, and UniProt lists its subcellular location as the cytoplasm. Alternatively spliced transcript variants encoding distinct isoforms have been identified.
BAG4 was found to associate with the death domain of tumour necrosis factor receptor type 1 (TNF-R1) and death receptor-3 (DR3), and in this way negatively regulates downstream cell death signalling. Its regulatory role in cell death was demonstrated in epithelial cells that undergo apoptosis when integrin-mediated matrix contacts are lost. The gene was previously named BCL2 associated athanogene 4, and the alias SODD is also used in the literature. A mouse ortholog, Bag4, is recorded.
BAG4 inhibits HSP70/HSC70 chaperone activity by promoting substrate release, making it a useful subject for studying cochaperone control of protein folding cycles.
BAG4 associates with the death domains of TNF-R1 and DR3 and prevents constitutive TNFRSF1A signalling, so it is studied in cell death pathways.
Its regulatory role was shown in epithelial cells undergoing apoptosis after loss of integrin-mediated matrix contacts.
BAG4 negatively regulates PRKN translocation to damaged mitochondria, linking it to research on mitochondrial damage responses.
BAG4 inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. It also prevents constitutive TNFRSF1A signalling and negatively regulates PRKN translocation to damaged mitochondria. Through binding the death domains of TNF-R1 and DR3, it dampens downstream cell death signalling.
Yes. SODD is an alias of BAG4. The gene's earlier HGNC name was BCL2 associated athanogene 4, and it is now named BAG cochaperone 4. The UniProt protein name is BAG family molecular chaperone regulator 4. Alternatively spliced transcript variants encoding distinct isoforms have been reported.
BAG4 is a member of the BAG1-related protein family and the BAG cochaperone gene group, sharing a C-terminal BAG domain that binds HSC70/HSP70. A mouse ortholog, Bag4, exists. Check the datasheet of any product for its validated reactivity.
Other BAG family cochaperones and related proteins involved in chaperone regulation and cell death signalling.
Gene and protein annotations from HGNC, NCBI Gene and UniProt O95429; product specifications from Assay Genie datasheets.