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Bcl2-associated athanogene 2

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 predicted BAG2 protein contains 211 amino acids. 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. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: catalase, HAD, CAN, ATPase, FasT
Papers on bag2
BAG2 expression dictates a functional intracellular switch between the p38-dependent effects of nicotine on tau phosphorylation levels via the α7 nicotinic receptor.
Carrettiero et al., São Bernardo do Campo, Brazil. In Exp Neurol, Jan 2016
The co-chaperone BAG2 is capable of regulating phospho-tau levels via protein degradation.
BAG2 Gene-mediated Regulation of PINK1 Protein Is Critical for Mitochondrial Translocation of PARKIN and Neuronal Survival.
Park et al., Ottawa, Canada. In J Biol Chem, Jan 2016
In this study, we identify Bcl2-associated athanogene 2 (BAG2) as a factor that promotes mitophagy.
BAG2 Is Repressed by NF-κB Signaling, and Its Overexpression Is Sufficient to Shift Aβ1-42 from Neurotrophic to Neurotoxic in Undifferentiated SH-SY5Y Neuroblastoma.
Carrettiero et al., São Bernardo do Campo, Brazil. In J Mol Neurosci, Sep 2015
The cochaperone BAG2 has been shown to mediate important cellular responses to stress, including cell cycle arrest and apoptosis.
The Co-chaperone BAG2 Mediates Cold-Induced Accumulation of Phosphorylated Tau in SH-SY5Y Cells.
Carrettiero et al., São Bernardo do Campo, Brazil. In Cell Mol Neurobiol, Aug 2015
Under the temperature of 37 °C, the co-chaperone BAG2 protein targets phosphorylated tau for degradation via by a more-efficient, ubiquitin-independent pathway.
CLIP2 as radiation biomarker in papillary thyroid carcinoma.
Hess et al., München, Germany. In Oncogene, Aug 2015
The genes comprising the first neighbourhood of CLIP2 (BAG2, CHST3, KIF3C, NEURL1, PPIL3 and RGS4) suggest the involvement of CLIP2 in the fundamental carcinogenic processes including apoptosis, mitogen-activated protein kinase signalling and genomic instability.
The BAG2 and BAG5 proteins inhibit the ubiquitination of pathogenic ataxin3-80Q.
Guo et al., Changsha, China. In Int J Neurosci, May 2015
Here, we report that BAG2 (Bcl-2 associated athanogene family protein 2) and BAG5 (Bcl-2-associated athanogene family protein 5) stabilise pathogenic ataxin3-80Q by inhibiting its ubiquitination as determined based on western blotting and co-immunofluorescence experiments.
The C. elegans UNC-23 protein, a member of the BCL-2-associated athanogene (BAG) family of chaperone regulators, interacts with HSP-1 to regulate cell attachment and maintain hypodermal integrity.
Moerman et al., Colombia. In Worm, Apr 2015
We have determined that the unc-23 gene product is the nematode ortholog of the human BAG-2 protein, a member of the Bcl-2 associated athanogene (BAG) family of molecular chaperone regulators.
Bcl-2-associated athanogene 2 prevents the neurotoxicity of MPP+ via interaction with DJ-1.
Zhang et al., China. In J Mol Neurosci, Mar 2015
Bcl-2-associated athanogene 2 (BAG2) is an important member in the BAG family which is characterized by their property of interaction with a variety of partners involved in modulating the proliferation/death balance.
BAG2 promotes tumorigenesis through enhancing mutant p53 protein levels and function.
Hu et al., New Brunswick, United States. In Elife, 2014
Here, we found that BAG2, a protein of Bcl-2 associated athanogene (BAG) family, promotes mutp53 accumulation and GOF in tumors.
Involvement of Bcl-2-associated athanogene (BAG)-family proteins in the neuroprotection by rasagiline.
Tang et al., Changsha, China. In Int J Clin Exp Med, 2014
We found that after the administration of 1-methy1-4-phenvl-1,2,3,6-tetrahvdropvridine (MPTP), BAG2 and BAG5 proteins were up-regulated in the substantia nigra dopaminergic neurons of PD mouse model.
Functions of MiRNA-128 on the regulation of head and neck squamous cell carcinoma growth and apoptosis.
Gu et al., Hangzhou, China. In Plos One, 2014
miRNA-128 was able to bind with the 3'-untranslated regions of BMI-1, BAG-2, BAX, H3f3b, and Paip2 mRNAs, resulting in significant reduction of the targeted protein levels.
Acclimatization to long-term hypoxia: gene expression in ovine carotid arteries.
Longo et al., Loma Linda, United States. In Physiol Genomics, 2014
Major upregulated genes included suprabasin and myelin basic protein, whereas downregulated genes included BAG2.
Crystallization and preliminary X-ray crystallographic analysis of the Bag2 amino-terminal domain from Mus musculus.
Misra et al., Cleveland, United States. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2012
Native Bag2-NTD crystals diffracted to 2.27 A resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 75.5, b = 84.7, c = 114.1 A
Regulation of energy homeostasis by bombesin receptor subtype-3: selective receptor agonists for the treatment of obesity.
Reitman et al., Rahway, United States. In Cell Metab, 2010
We developed potent, selective agonist (Bag-1, Bag-2) and antagonist (Bantag-1) ligands to explore BRS-3 function.
The cochaperone BAG2 sweeps paired helical filament- insoluble tau from the microtubule.
Kosik et al., Santa Barbara, United States. In J Neurosci, 2009
BAG2 levels in cells are under the physiological control of the microRNA miR-128a, which can tune paired helical filament Tau levels in neurons.
Structural basis of nucleotide exchange and client binding by the Hsp70 cochaperone Bag2.
Misra et al., Cleveland, United States. In Nat Struct Mol Biol, 2008
Free and Hsc70-bound crystal structures of Bag2-BNB show its dimeric structure, in which a flanking linker helix and loop bind to Hsc70 to promote nucleotide exchange.
BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP.
Höhfeld et al., Bonn, Germany. In Mol Biol Cell, 2005
The activity of BAG-2 resembles that of the previously characterized Hsc70 cochaperone and CHIP inhibitor HspBP1.
Regulation of the cytoplasmic quality control protein degradation pathway by BAG2.
Patterson et al., Chapel Hill, United States. In J Biol Chem, 2005
BAG2 binds to the carboxyl terminus of Hsp70-interacting protein (CHIP) and provides a cochaperone-dependent regulatory mechanism for preventing unregulated ubiquitylation of misfolded proteins by CHIP
Expression of myosin heavy chain isoforms and myogenesis of intrafusal fibres in rat muscle spindles.
Thornell et al., Praha, Czech Republic. In Microsc Res Tech, 1995
The three types of intrafusal fibres--nuclear bag1, nuclear bag2, and nuclear chain fibres--are unique in co-expressing several MHCs including special isoforms such as slow tonic and alpha cardiac-like MHC and isoforms typical of muscle development, such as embryonic and neonatal MHC.
Isolation, culture, and transplantation of rat hepatocytic precursor (stem-like) cells.
Smith et al., Chapel Hill, United States. In Proc Soc Exp Biol Med, 1993
When WB cells are tagged genetically with genes for bacterial beta-galactosidase and neomycin resistance (BAG2-WB), they and their progeny can be distinguished from parental WB cells and hepatocytes by the expression of these gene products.
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