BAF53/ACTL6 proteins are highly homologous, actin-related proteins found in the SWI/SNF complex. In addition to the canonical SWI/SNF complex, BAF53A/ACTL6A is also member of the embryonic SWI/SNF complex, known as esBAF, which plays a role in pluripotency and development. BAF53B/ACTL6B is a member of the neural-specific SWI/SNF complex that facilitates binding to target genes and is involved in memory and synaptic plasticity. BAF53/ACTL6 has been shown to interact with c-Myc, where it functions as a cofactor and is important in the transformation process. Further studies have shown ACTL6/BAF53 is associated with EMT and transformation in various cancers.
BAF60C, also known as SMARCD3, is a protein that is encoded by the SMARCD3 gene in human. BAF60C is a member of the SWI/SNF family of proteins, it displays helicase and ATPase activities and which are thought to regulate transcription of certain genes by altering the chromatin structure around those genes. BAF60C is part of the large ATP-dependent chromatin remodeling complex SNF/SWI and has sequence similarity to the yeast Swp73 protein. BAF60C together with TBX15 triggers development glycolytic fast-twitch muscles by the activation of the Akt/PKB signaling pathway.
BAG2, as one co-chaperone for HSP70 and HSC70 chaperone proteins, could act as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release.
BAG proteins compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. All the BAG proteins have an approximately 45-amino acid BAG domain near the C terminus but differ markedly in their N-terminal regions. The protein encoded by this gene contains a WW domain in the N-terminal region and a BAG domain in the C-terminal region. The BAG domains of BAG1, BAG2, and BAG3 interact specifically with the Hsc70 ATPase domain in vitro and in mammalian cells. All 3 proteins bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner.
The protein encoded by this gene belongs to the BCL2 protein family. BCL2 family members form oligomers or heterodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. This protein localizes to mitochondria, and functions to induce apoptosis. It interacts with and accelerates the opening of the mitochondrial voltage-dependent anion channel, which leads to a loss in membrane potential and the release of cytochrome c. This protein also interacts with the tumor suppressor P53 after exposure to cell stress.
This protein may play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi and be involved in CASP8-mediated apoptosis.
Functions as a chaperone protein. Is one of the most abundant endoplasmic reticulum (ER) proteins. Plays a role in the export of secreted proteins in the ER, the recognition of abnormally folded protein and their targeting to the ER associated-degradation (ERAD). Also serves as a cargo receptor for the export of transmembrane proteins. May be involved in CASP8-mediated apoptosis.
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