Affinage

BAG2

BAG family molecular chaperone regulator 2 · UniProt O95816

Length
211 aa
Mass
23.8 kDa
Annotated
2026-04-28
53 papers in source corpus 25 papers cited in narrative 25 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

BAG2 is an Hsc70/Hsp70 co-chaperone that functions as a central gatekeeper of protein quality control by coupling nucleotide exchange on Hsp70-family chaperones with potent inhibition of the CHIP/STUB1 E3 ubiquitin ligase, thereby diverting chaperone-bound clients from ubiquitin-dependent proteasomal degradation toward alternative fates including refolding, ubiquitin-independent 20S proteasomal degradation, and regulated stabilization. Structurally, BAG2 employs a dimeric 'brand new bag' (BNB) domain—distinct from canonical BAG domains—to promote nucleotide exchange on Hsc70, while its N-terminal domain blocks CHIP–E2 cooperation to suppress ubiquitination of diverse substrates including PINK1, STING, mutant p53, ERβ, HSP70 itself, and phospho-tau (PMID:19029896, PMID:16207813, PMID:26538564, PMID:26271008, PMID:40364789). Under stress, BAG2 undergoes liquid–liquid phase separation to form RNA-free condensates that recruit Hsp70 and the PA28-activated 20S proteasome for ubiquitin-independent client degradation, and it is phosphorylated by ULK1 at Ser31 to release AMBRA1 and initiate autophagy (PMID:35654899, PMID:39207901). BAG2 also functions as a direct arginine sensor through residue Q167, coupling amino-acid availability to β-catenin/ATF4 signaling via SAMD4B (PMID:40555234).

Mechanistic history

Synthesis pass · year-by-year structured walk · 11 steps
  1. 2005 High

    Establishing BAG2 as a CHIP inhibitor resolved how the chaperone-associated ubiquitin ligase could be negatively regulated, revealing that BAG2 forms a ternary complex with Hsc70 and CHIP to block E2 cooperation and client ubiquitination.

    Evidence Proteomic identification of BAG2 in CHIP complexes from HeLa cells; in vitro and in vivo ubiquitylation assays with misfolded CFTR as substrate; two independent labs

    PMID:16169850 PMID:16207813

    Open questions at the time
    • Structural basis for how BAG2 blocks CHIP-E2 interaction was unresolved
    • Whether BAG2 inhibits CHIP independently of Hsc70 was unclear
    • Range of endogenous clients affected in vivo was unknown
  2. 2008 High

    Crystal structures revealed that BAG2 uses a novel dimeric 'brand new bag' (BNB) domain to catalyze nucleotide exchange on Hsc70, establishing it as a structurally distinct class of Hsp70 NEF.

    Evidence X-ray crystallography of free and Hsc70-bound BAG2-BNB domain; NMR mapping of client- and Hsc70-binding sites; mutagenesis

    PMID:19029896

    Open questions at the time
    • Full-length BAG2 structure including the N-terminal CHIP-inhibitory domain was not determined
    • Whether dimerization is required for function in cells was untested
  3. 2009 High

    Discovery that BAG2-Hsp70 delivers phospho-tau to the proteasome for ubiquitin-independent degradation along microtubules established BAG2 as a clearance factor for neurodegenerative disease substrates, linking the co-chaperone to a non-canonical degradation route.

    Evidence Neuronal cell-based tau degradation assays; sarkosyl-insoluble tau fractionation; miR-128a manipulation of BAG2 levels

    PMID:19228967

    Open questions at the time
    • Identity of the proteasome complex (20S vs 26S) mediating ubiquitin-independent degradation was unresolved
    • In vivo relevance in tauopathy animal models was not shown
  4. 2013 Medium

    Identification of BAG2 as a stabilizer of PINK1 extended its client repertoire to mitochondrial quality control, showing that BAG2 inhibits PINK1 ubiquitination and prevents its proteasomal degradation.

    Evidence Co-immunoprecipitation and ubiquitination assays in cell lines; wild-type and pathogenic R492X PINK1 mutant

    PMID:24383081

    Open questions at the time
    • Whether BAG2-mediated PINK1 stabilization activates downstream mitophagy was untested
    • The E3 ligase responsible for PINK1 ubiquitination blocked by BAG2 was not identified
  5. 2015 High

    Two parallel advances showed that BAG2's anti-ubiquitination function has opposing biological consequences depending on the client: stabilization of PINK1 triggers protective PARKIN-dependent mitophagy in neurons, while stabilization of mutant p53 promotes oncogenic gain-of-function by blocking MDM2-mediated degradation.

    Evidence PINK1: mitophagy assays, MPP+ neuroprotection, KD/OE (PMID:26538564); mutant p53: nuclear fractionation, MDM2-mutp53 interaction assays, mouse tumor xenografts (PMID:26271008)

    PMID:26271008 PMID:26538564

    Open questions at the time
    • Whether BAG2 uses the same structural interface to block both MDM2 and CHIP was unknown
    • Tissue-specific regulation determining which client dominates was unexplored
  6. 2016 High

    Genetic epistasis in C. elegans placed the BAG2-Hsc70 complex upstream of LRRK2/LRK-1 in polarized axonal protein sorting at the Golgi, extending BAG2 function beyond protein degradation to chaperone-dependent membrane protein trafficking.

    Evidence C. elegans suppressor genetics with unc-23 (BAG2 ortholog) and hsp-1 alleles; fluorescence imaging of synaptic vesicle protein mislocalization

    PMID:26853528

    Open questions at the time
    • Biochemical mechanism by which BAG2-Hsc70 regulates LRRK2 Golgi localization was unknown
    • Relevance to mammalian LRRK2-linked Parkinson's disease was not tested
  7. 2017 High

    BAG2 was shown to regulate pro-cathepsin B processing and vesicular trafficking to the cell surface, revealing a role in secretory pathway-dependent tumor metastasis independent of its CHIP-inhibitory function.

    Evidence Co-IP of BAG2 with pro-cathepsin B propeptide; TGN38-positive vesicle trafficking assays; mouse xenografts in triple-negative breast cancer

    PMID:29212038

    Open questions at the time
    • Whether Hsp70 NEF activity is required for cathepsin B trafficking was not determined
    • Direct versus chaperone-mediated binding of BAG2 to pro-cathepsin B was not resolved
  8. 2022 High

    The discovery that BAG2 undergoes liquid–liquid phase separation under stress to form RNA-free condensates containing Hsp70 and PA28-activated 20S proteasome provided the mechanistic basis for ubiquitin-independent client degradation first observed with tau in 2009.

    Evidence Live-cell imaging; in vitro phase separation assays; proteasome inhibition; co-localization with tau; microtubule-dependent trafficking

    PMID:35654899

    Open questions at the time
    • Structural determinants within BAG2 driving phase separation were not mapped
    • Whether condensate-mediated degradation operates in vivo in disease tissues was untested
    • Selectivity of client recruitment into condensates was unclear
  9. 2024 High

    Phosphorylation of BAG2 at Ser31 by ULK1 was identified as a switch that releases the autophagy regulator AMBRA1, connecting BAG2 to starvation-induced autophagy initiation and revealing BAG2 as a direct effector of the ULK1 kinase complex.

    Evidence AP-MS and proximity labeling-MS; phospho-site mutagenesis (S31A/S31E); AMBRA1 ER relocalization imaging; autophagy flux assays

    PMID:39207901

    Open questions at the time
    • How BAG2's chaperone and CHIP-inhibitory functions intersect with its autophagy role was not addressed
    • Whether Ser31 phosphorylation affects BAG2 condensate formation was unknown
  10. 2025 High

    BAG2 was identified as a direct arginine sensor through residue Q167, coupling amino-acid availability to β-catenin stability and ATF4-dependent stress adaptation via SAMD4B—a function entirely independent of its chaperone co-factor role.

    Evidence Unbiased screening; direct arginine-binding assays; Q167 mutagenesis; SAMD4B Co-IP; β-catenin/ATF4 protein level measurements

    PMID:40555234

    Open questions at the time
    • Whether arginine sensing requires or is modulated by Hsp70 binding was not tested
    • Structural basis of arginine recognition at Q167 awaits high-resolution characterization
    • In vivo physiological contexts for arginine sensing by BAG2 were not established
  11. 2025 Medium

    BAG2 was shown to inhibit CHIP-mediated K48-ubiquitination of STING at specific lysine residues and to interact with WDR62 to regulate HPRT turnover, broadening the client repertoire to innate immunity signaling and purine metabolism.

    Evidence STING: ubiquitination assays with K338R/K370R mutants, IFN pathway readouts (PMID:40364789); WDR62: proximity ligation, BAG2 KD in WDR62-KO cells, HPRT stability assays (PMID:41787126)

    PMID:40364789 PMID:41787126

    Open questions at the time
    • Whether BAG2-STING interaction is direct or Hsp70-mediated was not determined
    • Mechanism by which WDR62 restrains BAG2-dependent HPRT degradation is unknown
    • Both findings from single labs without independent replication

Open questions

Synthesis pass · forward-looking unresolved questions
  • A unified structural model integrating BAG2's BNB domain (NEF), N-terminal CHIP-inhibitory region, phase-separation determinants, ULK1 phosphosite, and arginine-sensing residue is lacking, leaving open how these distinct functions are coordinated and whether they are mutually exclusive or coexist in different cellular compartments.
  • Full-length BAG2 structure is unavailable
  • Compartment-specific BAG2 interactome has not been mapped
  • In vivo genetic models (conditional knockout) with multi-organ phenotyping have not been reported

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 6 GO:0044183 protein folding chaperone 2 GO:0060090 molecular adaptor activity 1 GO:0140299 molecular sensor activity 1
Localization
GO:0005829 cytosol 3 GO:0005856 cytoskeleton 2 GO:0005634 nucleus 1 GO:0005794 Golgi apparatus 1
Pathway
R-HSA-392499 Metabolism of proteins 8 R-HSA-9612973 Autophagy 3 R-HSA-1852241 Organelle biogenesis and maintenance 2 R-HSA-162582 Signal Transduction 1 R-HSA-168256 Immune System 1
Partners
AMBRA1HSPA8PINK1SAMD4BSTUB1TMEM173TP53WDR62
Complex memberships
BAG2-Hsc70-CHIP ternary complexBAG2-Hsp70-20S/PA28 condensate

Evidence

Reading pass · 25 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2005 BAG2 is a component of CHIP-containing protein complexes in human cells and inhibits the ubiquitin ligase activity of CHIP by abrogating CHIP/E2 (UbcH5a) cooperation, thereby preventing ubiquitination of chaperone-presented client proteins such as misfolded CFTR and stimulating chaperone-assisted maturation. Peptide mass fingerprinting of CHIP complexes from HeLa cells; in vitro and in vivo ubiquitylation assays; binding assays demonstrating ternary BAG2-Hsc70-CHIP complex Molecular biology of the cell High 16169850 16207813
2005 BAG2 associates with CHIP as part of a ternary complex with Hsc70, and ATP-dependent remodeling of the BAG2-Hsc70-CHIP heterocomplex may facilitate inhibition of CHIP-dependent ubiquitin ligase activity; BAG2 colocalizes with CHIP under quiescent conditions and after heat shock. Proteomics (in vivo complex identification); binding assays; in vitro and in vivo ubiquitylation assays; colocalization studies The Journal of biological chemistry High 16169850
2008 BAG2 contains a novel Hsp70 nucleotide-exchange factor (NEF) domain called the 'brand new bag' (BNB) domain, distinct from canonical BAG domains. Crystal structures of free and Hsc70-bound BAG2-BNB reveal a dimeric architecture where a flanking linker helix and loop bind Hsc70 to promote nucleotide exchange. NMR shows client-binding sites overlap with Hsc70-interaction sites, and Hsc70 can displace clients from BAG2-BNB. X-ray crystallography (free and Hsc70-bound structures); NMR analysis; mutagenesis Nature structural & molecular biology High 19029896
2009 The BAG2/Hsp70 complex is tethered to microtubules, where it captures and delivers tau (preferentially sarkosyl-insoluble and phosphorylated tau) to the proteasome for ubiquitin-independent degradation. BAG2 levels in neurons are regulated by microRNA miR-128a, which tunes PHF-tau levels. Cell-based assays; fractionation; knockdown/overexpression with tau degradation readouts; miRNA manipulation The Journal of neuroscience High 19228967
2013 BAG2 directly binds PINK1 and stabilizes it by decreasing its ubiquitination, thereby preventing proteasomal degradation of PINK1. BAG2 also binds the pathogenic R492X PINK1 mutant and stabilizes it to a greater extent than wild-type PINK1. Co-immunoprecipitation; western blotting; ubiquitination assays Biochemical and biophysical research communications Medium 24383081
2015 BAG2 inhibits PINK1 degradation by blocking ubiquitination, which stabilizes PINK1 on depolarized mitochondria, triggers PARKIN-mediated mitophagy, and protects neurons against MPP+-induced oxidative stress. BAG2 is thus an upstream regulator of the PINK1/PARKIN signaling pathway. Cell-based PINK1 stabilization assays; mitophagy assays; neuronal protection assays (MPP+ model); BAG2 knockdown/overexpression The Journal of biological chemistry High 26538564
2015 BAG2 binds mutant p53 (mutp53) and translocates to the nucleus to inhibit MDM2-mutp53 interaction and MDM2-mediated ubiquitination and degradation of mutp53, thereby promoting mutp53 accumulation and gain-of-function in tumor growth, metastasis, and chemoresistance. Co-immunoprecipitation; ubiquitination assays; nuclear fractionation; loss-of-function/gain-of-function studies in tumor cells and mouse models eLife High 26271008
2016 BAG2 inhibits CHIP-mediated ubiquitination of HSP72, preventing its degradation; in aged/senescent human fibroblasts, increased BAG2 levels functionally counteract increased CHIP levels to maintain reduced HSP72 ubiquitination. In vitro ubiquitination assays; western blotting; primary human fibroblast gain/loss-of-function International journal of molecular sciences Medium 28042827
2016 The BAG2-HSC70 chaperone complex regulates Golgi localization of LRRK2/LRK-1 in C. elegans neurons; loss of UNC-23 (BAG2 ortholog) or HSP-1 (Hsc70) causes missorting of synaptic vesicle proteins, phenocopying lrk-1 deletion. HSP-1 mutations suppress unc-23 but not lrk-1 defects, placing BAG2-Hsc70 upstream of LRK-1 in polarized axonal sorting. C. elegans genetics; epistasis analysis; fluorescence microscopy of neuronal protein localization; yeast two-hybrid Genes to cells High 26853528
2017 BAG2 interacts with the propeptide region of pro-cathepsin B via Co-IP and blocks its auto-cleavage processing; BAG2 also regulates pro-cathepsin B/annexin II complex formation and facilitates trafficking of pro-cathepsin B-containing TGN38-positive vesicles to the cell periphery for secretion, promoting metastasis in triple-negative breast cancer. Co-immunoprecipitation; siRNA knockdown; vesicle trafficking assays; in vitro processing assays; mouse xenograft models Cell reports High 29212038
2018 BAG2 (acting as an Hsc70 nucleotide-exchange factor) stimulates SV40 release from Hsc70, enabling the virus to reach the cytosol from the ER during nonenveloped polyomavirus infection. This was shown by demonstrating that Bag2 promotes SV40 ejection from the Hsc70-SGTA-Hsp105 cytosolic extraction complex. Viral infection assays; Co-IP of Hsc70-Bag2 interaction; NEF activity assay; dominant-negative and knockdown approaches Journal of virology Medium 29769335
2019 BAG2 overexpression in M. tuberculosis-infected macrophages activates autophagic flux and reticulophagy (ER-targeted autophagy) by localizing SQSTM1/p62 to the ER; BAG2-activated autophagy is mediated through MAPK/ERK-dependent dissociation of BECN1 from BCL2. XBP1, downstream of IRE1 signaling, transcriptionally represses BAG2 expression via binding to the BAG2 promoter. BAG2 overexpression; autophagic flux assays; chromatin immunoprecipitation (XBP1-BAG2 promoter binding); co-immunoprecipitation (BECN1-BCL2); immunofluorescence Autophagy Medium 31711362
2020 LOXL1 interacts with BAG2-K186 via a hydrogen bond through LOXL1-D515, and LOXL1's lysyl oxidase activity prevents BAG2 degradation by competing with K186 ubiquitylation, thereby stabilizing BAG2 protein levels in glioma cells. Co-immunoprecipitation; ubiquitination assays; site-directed mutagenesis (LOXL1-D515, BAG2-K186); gain/loss-of-function Cell death and differentiation Medium 32424143
2021 BAG2 inhibits CHIP-mediated ubiquitin-proteasomal degradation of ERβ (but not ERα) in endometrial stromal cells, thereby modulating estrogen receptor status in endometriosis; knockdown of both BAG2 and MDM2 alleviated endometriosis development in mice. HA-/FLAG-immunoprecipitation; immunoblotting with anti-ubiquitin antibody; mouse endometriosis model; HESC isolation and knockdown Frontiers in cell and developmental biology Medium 33987175
2022 USP49, transcriptionally activated by c-MYC in colorectal cancer, deubiquitinates and stabilizes BAG2 protein, defining a c-MYC-USP49-BAG2 axis that promotes cancer cell survival. Co-immunoprecipitation; ubiquitination assays; deubiquitinase activity assays; KD with proliferation/apoptosis readouts Biochemical and biophysical research communications Medium 35367823
2022 Under stress (particularly hyper-osmotic stress), BAG2 forms phase-separated, RNA-free, ubiquitin-free membraneless organelles (condensates) that promote ubiquitin-independent client protein degradation via the 20S proteasome. These condensates contain Hsp70 and 20S proteasome activated by PA28 family members, can traffic along microtubules to tau, and, when proteasome is inhibited, traffic to aggresome-like structures. Live-cell imaging; phase separation assays; immunofluorescence; proteasome inhibition; co-localization with stress granule/P-body markers; tau degradation assays Nature communications High 35654899
2023 BAG2 localizes in mutant p53 aggregates, interacts with misfolded p53 mutants, exacerbates aggregate formation, and recruits HSP90 to promote propagation and maintenance of mutant p53 aggregates, thereby inhibiting mitochondrial apoptosis and causing chemoresistance in breast cancer. Co-immunoprecipitation; immunofluorescence; semi-denaturing detergent-agarose gel electrophoresis; KD/OE in cell lines and mouse models Theranostics Medium 36593950
2024 BAG2 is an effector of the ULK1 kinase complex; in growth conditions, unphosphorylated BAG2 sequesters AMBRA1 to attenuate autophagy induction. Under starvation, ULK1 phosphorylates BAG2 at Ser31, which releases AMBRA1 and supports its recruitment to the ER membrane, promoting autophagy initiation. Affinity purification-mass spectrometry; proximity labeling-MS; phosphorylation site mutagenesis; AMBRA1 localization by imaging; autophagy flux assays Cell reports High 39207901
2024 In fibrolamellar carcinoma, DNAJ-PKAc fusion kinase phosphorylates BAG2; BAG2 is recruited to the DNAJ-PKAc scaffold through its association with Hsp70, and the DNAJ-PKAc/Hsp70/BAG2 axis contributes to chemotherapeutic resistance. Proximity proteomics; biochemical Co-IP; live-cell photoactivation microscopy; pharmacological inhibition; patient tissue immunoblot/IHC Cell reports Medium 38236773
2024 Bag2 maintains PINK1 protein stability by binding PINK1 and protecting it from proteasome-dependent degradation in cardiomyocytes, thereby preserving mitophagy activation and protecting against doxorubicin-induced cardiotoxicity. Co-immunoprecipitation; proteasome inhibition assays; gain/loss-of-function in cells and C57BL/6 mice; mitophagy assays Toxicology Medium 39442788
2025 BAG2 functions as a direct arginine sensor, binding arginine at glutamine residue Q167. When arginine is deficient, BAG2 releases SAMD4B, leading to β-catenin degradation and ATF4 stabilization to enhance cell survival. When arginine is abundant, BAG2-SAMD4B interaction is strengthened, preventing β-catenin degradation and activating Wnt/β-catenin signaling for cell growth. Unbiased screening; direct arginine-binding assays; mutagenesis (Q167); Co-IP of BAG2-SAMD4B; β-catenin/ATF4 protein level assays; loss-of-function studies Molecular cell High 40555234
2025 BAG2 interacts directly with WDR62, a microcephaly scaffold protein, and co-localizes with it in cytoplasmic granules under stress. In WDR62-deficient cells, elevated BAG2 levels destabilize HPRT (a purine salvage enzyme); BAG2 knockdown in WDR62-deficient cells restores HPRT levels, indicating BAG2 promotes HPRT turnover when not regulated by WDR62. Co-immunoprecipitation; proximity-ligation; BAG2 knockdown in WDR62-KO cells; HPRT stability assays; imaging of stress-induced granules The EMBO journal Medium 41787126
2025 BAG2 inhibits STUB1/CHIP-mediated K48-linked ubiquitination of STING at K338 and K370 by forming a complex with STUB1, thereby stabilizing STING protein and activating the type I interferon pathway in cervical cancer cells. Co-immunoprecipitation; ubiquitination assays with site-specific mutants (K338R, K370R); BAG2 KD/OE; IFN pathway readouts; patient tissue analysis Advanced science Medium 40364789
2025 BAG2 interacts with CHIP to inhibit ubiquitination and degradation of HSP70, maintaining elevated HSP70 levels that bind Apaf1, reduce cytochrome C release from mitochondria, and thereby block apoptosome assembly and inhibit apoptosis in gastric cancer cells. Co-immunoprecipitation; ubiquitination assays; KD/OE with apoptosis readouts; cytochrome C release assays; Apaf1-HSP70 interaction assays Frontiers in immunology Medium 40755756
2014 BAG2 inhibits ubiquitination of pathogenic polyglutamine-expanded ataxin3-80Q (SCA3 mutant), stabilizing the protein; this was shown by co-immunoprecipitation and co-immunofluorescence. Co-immunoprecipitation; co-immunofluorescence; ubiquitination western blot The International journal of neuroscience Low 25006867

Source papers

Stage 0 corpus · 53 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2005 BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP. Molecular biology of the cell 166 16207813
2009 The cochaperone BAG2 sweeps paired helical filament- insoluble tau from the microtubule. The Journal of neuroscience : the official journal of the Society for Neuroscience 138 19228967
2005 Regulation of the cytoplasmic quality control protein degradation pathway by BAG2. The Journal of biological chemistry 127 16169850
2008 Structural basis of nucleotide exchange and client binding by the Hsp70 cochaperone Bag2. Nature structural & molecular biology 82 19029896
2016 BAG2 structure, function and involvement in disease. Cellular & molecular biology letters 68 28536620
2015 BAG2 promotes tumorigenesis through enhancing mutant p53 protein levels and function. eLife 68 26271008
2019 BAG2 ameliorates endoplasmic reticulum stress-induced cell apoptosis in Mycobacterium tuberculosis-infected macrophages through selective autophagy. Autophagy 54 31711362
2015 BAG2 Gene-mediated Regulation of PINK1 Protein Is Critical for Mitochondrial Translocation of PARKIN and Neuronal Survival. The Journal of biological chemistry 54 26538564
2017 Co-chaperone BAG2 Determines the Pro-oncogenic Role of Cathepsin B in Triple-Negative Breast Cancer Cells. Cell reports 46 29212038
2013 Curcumin-induced upregulation of the anti-tau cochaperone BAG2 in primary rat cortical neurons. Neuroscience letters 46 24035895
2022 Stress routes clients to the proteasome via a BAG2 ubiquitin-independent degradation condensate. Nature communications 42 35654899
2020 LOXL1 confers antiapoptosis and promotes gliomagenesis through stabilizing BAG2. Cell death and differentiation 41 32424143
2008 Induction of BAG2 protein during proteasome inhibitor-induced apoptosis in thyroid carcinoma cells. British journal of pharmacology 35 18660828
2013 The BAG2 protein stabilises PINK1 by decreasing its ubiquitination. Biochemical and biophysical research communications 32 24383081
2020 BAG2 Promotes Proliferation and Metastasis of Gastric Cancer via ERK1/2 Signaling and Partially Regulated by miR186. Frontiers in oncology 29 32082999
2020 Identification of BAG2 and Cathepsin D as Plasma Biomarkers for Parkinson's Disease. Clinical and translational science 29 33202088
2021 The BAG2 and BAG6 Genes Are Involved in Multiple Abiotic Stress Tolerances in Arabidopsis Thaliana. International journal of molecular sciences 26 34072612
2023 BAG2 drives chemoresistance of breast cancer by exacerbating mutant p53 aggregate. Theranostics 25 36593950
2022 c-MYC-USP49-BAG2 axis promotes proliferation and chemoresistance of colorectal cancer cells in vitro. Biochemical and biophysical research communications 24 35367823
2018 Bag2 Is a Component of a Cytosolic Extraction Machinery That Promotes Membrane Penetration of a Nonenveloped Virus. Journal of virology 23 29769335
2015 The Co-chaperone BAG2 Mediates Cold-Induced Accumulation of Phosphorylated Tau in SH-SY5Y Cells. Cellular and molecular neurobiology 20 26208804
2011 BAG2 is a target of the c-Myc gene and is involved in cellular senescence via the p21(CIP1) pathway. Cancer letters 19 22146591
2016 BAG2 Interferes with CHIP-Mediated Ubiquitination of HSP72. International journal of molecular sciences 18 28042827
2021 BAG2-Mediated Inhibition of CHIP Expression and Overexpression of MDM2 Contribute to the Initiation of Endometriosis by Modulating Estrogen Receptor Status. Frontiers in cell and developmental biology 17 33987175
2023 GNB1 promotes hepatocellular carcinoma progression by targeting BAG2 to activate P38/MAPK signaling. Cancer science 14 36718954
2015 BAG2 expression dictates a functional intracellular switch between the p38-dependent effects of nicotine on tau phosphorylation levels via the α7 nicotinic receptor. Experimental neurology 14 26496817
2024 Recruitment of BAG2 to DNAJ-PKAc scaffolds promotes cell survival and resistance to drug-induced apoptosis in fibrolamellar carcinoma. Cell reports 13 38236773
2016 Chaperone complex BAG2-HSC70 regulates localization of Caenorhabditis elegans leucine-rich repeat kinase LRK-1 to the Golgi. Genes to cells : devoted to molecular & cellular mechanisms 13 26853528
2024 The ULK1 effector BAG2 regulates autophagy initiation by modulating AMBRA1 localization. Cell reports 12 39207901
2015 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. Journal of molecular neuroscience : MN 11 25985852
2014 The BAG2 and BAG5 proteins inhibit the ubiquitination of pathogenic ataxin3-80Q. The International journal of neuroscience 11 25006867
2023 The relationship between protein modified folding molecular network and Alzheimer's disease pathogenesis based on BAG2-HSC70-STUB1-MAPT expression patterns analysis. Frontiers in aging neuroscience 9 37251806
2018 The role of Bag2 in neurotoxicity induced by the anesthetic sevoflurane. Journal of cellular biochemistry 9 30548665
2025 BAG2 releases SAMD4B upon sensing of arginine deficiency to promote tumor cell survival. Molecular cell 8 40555234
2022 BAG2 prevents Tau hyperphosphorylation and increases p62/SQSTM1 in cell models of neurodegeneration. Molecular biology reports 8 35612780
2021 MicroRNA-325 inhibits the proliferation and induces the apoptosis of T cell acute lymphoblastic leukemia cells in a BAG2-dependent manner. Experimental and therapeutic medicine 8 33936287
2021 Metastasis Risk Assessment Using BAG2 Expression by Cancer-Associated Fibroblast and Tumor Cells in Patients with Breast Cancer. Cancers 8 34572878
2025 BAG2 mediates HsfA1a-induced thermotolerance by regulating heat shock proteins in tomato. The Plant journal : for cell and molecular biology 7 40324163
2012 Crystallization and preliminary X-ray crystallographic analysis of the Bag2 amino-terminal domain from Mus musculus. Acta crystallographica. Section F, Structural biology and crystallization communications 7 22684061
2021 BAG2 mediates coelomocyte apoptosis in Vibrio splendidus challenged sea cucumber Apostichopus japonicus. International journal of biological macromolecules 6 34418417
2025 BAG2 Inhibits Cervical Cancer Progression by Modulating Type I Interferon Signaling through Stabilizing STING. Advanced science (Weinheim, Baden-Wurttemberg, Germany) 4 40364789
2024 Comparative analysis of BAG1 and BAG2: Insights into their structures, functions and implications in disease pathogenesis. International immunopharmacology 4 39405938
2023 CircRNA254 functions as the miR-375 sponge to inhibit coelomocyte apoptosis via targeting BAG2 in V. splendidus-challenged Apostichopus japonicus. Fish & shellfish immunology 4 37709179
2022 BAG2-activated cell autophagy and mir-27b dynamic regulation mechanism during Mycobacterium tuberculosis infection. Cellular and molecular biology (Noisy-le-Grand, France) 2 35818274
2025 Targeting the BAG2/CHIP axis promotes gastric cancer apoptosis by blocking apoptosome assembly. Frontiers in immunology 1 40755756
2024 Proteomic Analysis of HepG2 Cells Reveals FAT10 and BAG2 Signaling Pathways Affected by a Protease Inhibitor from Tinospora cordifolia (Willd.) Hook. f. and Thoms Stem. Extract Among the Different Plant and Microbial Samples Analyzed. Turkish journal of pharmaceutical sciences 1 38994797
2024 BAG2, MAD2L1, and MDK are cancer-driver genes and candidate targets for novel therapies in malignant pleural mesothelioma. Cancer gene therapy 1 39300217
2024 Bag2 protects against doxorubicin-induced cardiotoxicity by maintaining Pink1-mediated mitophagy. Toxicology 1 39442788
2026 Microcephaly-associated protein WDR62 supports purine metabolism by interacting with co-chaperone BAG2. The EMBO journal 0 41787126
2025 Disruption of Hsp70.14-BAG2 Protein-Protein interactions using deep Learning-Driven peptide design and molecular simulations. Computers in biology and medicine 0 40466244
2025 Therapeutic Potential of Compounds with High Affinity to BAG2 in Inhibiting Keloid Disease. Biologics : targets & therapy 0 40893173
2025 XLOC_010588 Promotes Mitophagy Via BAG2-Mediated PINK1 Stabilization in HPH. Hypertension (Dallas, Tex. : 1979) 0 41332376
2023 Recruitment of BAG2 to DNAJ-PKAc scaffolds promotes cell survival and resistance to drug-induced apoptosis in fibrolamellar carcinoma. bioRxiv : the preprint server for biology 0 37425703