Affinage

BAG2

BAG family molecular chaperone regulator 2 · UniProt O95816

Length
211 aa
Mass
23.8 kDa
Annotated
2026-06-09
54 papers in source corpus 26 papers cited in narrative 26 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

BAG2 is an Hsp70/Hsc70 co-chaperone and nucleotide-exchange factor that governs whether chaperone-bound client proteins are committed to ubiquitin-dependent degradation or rescued from it, thereby acting as a switch in protein quality control (PMID:16207813, PMID:16169850, PMID:19029896). Structurally it uses a distinct dimeric 'brand new bag' (BNB) nucleotide-exchange domain whose Hsc70-interaction and client-binding surfaces overlap, allowing Hsc70 to displace clients and driving ADP–ATP exchange during folding cycles (PMID:19029896). Functionally, BAG2 assembles into a ternary complex with Hsc70 and the E3 ligase CHIP/STUB1 and inhibits CHIP ubiquitin ligase activity by abrogating CHIP/E2 cooperation, a remodeling step facilitated by ATP (PMID:16207813, PMID:16169850). Through this CHIP-antagonizing activity—and analogous blockade of other ligases—BAG2 stabilizes a broad set of clients including HSP72/HSP70, misfolded CFTR, tau, mutant p53, PINK1, ERβ, and STING, redirecting clients such as tau toward ubiquitin-independent 20S proteasomal degradation (PMID:16207813, PMID:16169850, PMID:19228967, PMID:26271008, PMID:28042827, PMID:40364789). BAG2 forms stress-induced, RNA- and ubiquitin-free phase-separated condensates on microtubules that recruit HSP-70 and PA28/PSME proteasome activators and promote ubiquitin-independent client degradation, trafficking to tau or to aggresome-like structures when the proteasome is blocked (PMID:35654899). BAG2 also integrates nutrient and stress signaling: it is an effector of the ULK1 kinase complex phosphorylated on Ser31 to release AMBRA1 and license autophagy initiation (PMID:39207901), and it is a direct intracellular arginine sensor binding arginine at Q167 to control SAMD4B release and the balance between Wnt/β-catenin and ATF4 signaling (PMID:40555234). These activities position BAG2 as a recurrent determinant of cell survival, with stabilization of mutant p53, HSP70, and other clients driving chemoresistance and tumor progression across multiple cancers (PMID:26271008, PMID:36593950, PMID:40755756).

Mechanistic history

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

    Establishing how BAG2 enters protein quality control: it was unknown what restrained CHIP ubiquitin ligase activity on chaperone-bound clients, and BAG2 was identified as a CHIP-complex component that inhibits CHIP by blocking E2 cooperation and rescues clients like misfolded CFTR.

    Evidence Peptide mass fingerprinting of CHIP complexes with in vitro/in vivo ubiquitylation and binding assays in HeLa cells

    PMID:16169850 PMID:16207813

    Open questions at the time
    • Did not resolve which clients are universally protected versus rerouted
    • Mechanism of E2 exclusion not structurally defined at this stage
  2. 2005 High

    Defining the working assembly: BAG2 was shown to act within a ternary Hsc70-BAG2-CHIP heterocomplex whose ATP-dependent remodeling underlies CHIP inhibition, linking BAG2's chaperone association to its ligase-regulatory role.

    Evidence Co-IP, binding assays, and in vitro/in vivo ubiquitylation assays

    PMID:16169850 PMID:16207813

    Open questions at the time
    • Stoichiometry and dynamics of the heterocomplex unresolved
    • How ATP remodeling translates to E2 exclusion not defined
  3. 2008 High

    Resolving the molecular basis of BAG2's chaperone activity: the structurally novel dimeric BNB nucleotide-exchange domain was defined, showing overlapping client- and Hsc70-binding surfaces so that Hsc70 displaces clients, a distinct mode of regulating Hsp70 folding cycles.

    Evidence X-ray crystallography of free and Hsc70-bound BNB, NMR, and functional nucleotide-exchange assays

    PMID:19029896

    Open questions at the time
    • Structural basis for CHIP inhibition not captured
    • Link between NEF activity and condensate formation untested
  4. 2009 Medium

    Connecting BAG2 to neurodegeneration substrate clearance: it was unclear how phosphorylated/insoluble tau is removed, and the microtubule-tethered BAG2/Hsp70 complex was shown to capture and deliver tau to the proteasome for ubiquitin-independent degradation.

    Evidence Cellular localization, knockdown, and tau degradation assays in neurons

    PMID:19228967

    Open questions at the time
    • No full reconstitution of the degradation step
    • Single lab; proteasome species engaged not defined here
  5. 2015 Medium

    Extending the stabilization principle to disease-relevant clients: BAG2 was shown to bind PINK1, mutant p53, and HSP72 and block their ubiquitination, thereby driving mitophagy, oncogenic mutp53 gain-of-function, and counteracting age-related CHIP increases.

    Evidence Co-IP, ubiquitination assays, mitophagy and xenograft assays, primary fibroblasts

    PMID:24383081 PMID:26271008 PMID:26538564 PMID:28042827

    Open questions at the time
    • Whether stabilization is direct ligase inhibition or competitive shielding varies by client
    • In vivo relevance of mutp53 stabilization in patient tumors not addressed
  6. 2017 Medium

    Revealing chaperone-independent trafficking and secretion roles: BAG2 was found to bind the pro-cathepsin B propeptide, block its maturation, and promote vesicular trafficking and secretion driving breast cancer metastasis.

    Evidence Co-IP, vesicle trafficking assays, BAG2 silencing with metastasis readouts, fluorescence microscopy

    PMID:29212038

    Open questions at the time
    • Whether this requires Hsc70 co-chaperone activity unclear
    • Single lab
  7. 2018 Medium

    Placing BAG2 in extraction and viral entry pathways: as a NEF within a cytosolic Hsc70-SGTA-Hsp105 extraction complex, BAG2 stimulates SV40 release from Hsc70 to enable cytosolic arrival and infection.

    Evidence Virus infection assays, BAG2 depletion, biochemical fractionation, rescue

    PMID:29769335

    Open questions at the time
    • Direct biochemical contribution of BAG2 NEF activity to extraction not isolated
    • Single lab
  8. 2022 High

    Reframing BAG2 as a condensate scaffold: it marks stress-induced, RNA- and ubiquitin-free phase-separated granules containing HSP-70 and PA28/PSME that drive ubiquitin-independent 20S degradation and traffic on microtubules to tau or aggresomes.

    Evidence Live-cell fluorescence microscopy, phase separation assays, proteasome inhibition, fractionation

    PMID:35654899

    Open questions at the time
    • Sequence determinants of BAG2 phase separation not mapped
    • Relationship of condensates to the CHIP-inhibitory complex unresolved
  9. 2024 High

    Integrating BAG2 into autophagy signaling: it was unknown how BAG2 connects to autophagy machinery, and BAG2 was defined as a ULK1 effector phosphorylated on Ser31 that releases AMBRA1 to license autophagy initiation upon starvation.

    Evidence APMS/proximity labeling, ULK1 kinase assays, Ser31 mutagenesis, AMBRA1 localization and autophagy flux assays

    PMID:39207901

    Open questions at the time
    • Whether Ser31 phosphorylation affects co-chaperone or condensate functions untested
    • Structural basis of BAG2-AMBRA1 sequestration unknown
  10. 2025 High

    Establishing BAG2 as a nutrient sensor: an unbiased screen identified BAG2 as a direct intracellular arginine sensor binding at Q167, governing SAMD4B release and the Wnt/β-catenin versus ATF4 decision according to arginine status.

    Evidence Unbiased screening in cancer cell lines, biochemical binding assays, Q167 mutagenesis, Co-IP, signaling readouts

    PMID:40555234

    Open questions at the time
    • How arginine binding relates to co-chaperone or condensate functions unresolved
    • Physiological tissues where this sensing operates not defined
  11. 2025 Medium

    Broadening the client-stabilization repertoire and disease links: BAG2-STUB1 complexes block K48 ubiquitination of STING (K338/K370) to activate type I interferon, and BAG2 interacts with the microcephaly protein WDR62 to control HPRT stability, tying BAG2 to immunity and a Mendelian disorder.

    Evidence Co-IP, site-directed mutagenesis of ubiquitination sites, ubiquitination and interferon assays; WDR62 mutant rescue and HPRT stability assays

    PMID:40364789 PMID:41787126

    Open questions at the time
    • WDR62-BAG2 axis tested in cell models; in vivo microcephaly mechanism not established
    • Single lab for each axis

Open questions

Synthesis pass · forward-looking unresolved questions
  • How BAG2's distinct activities—CHIP/E2 inhibition, NEF cycling, microtubule condensate formation, ULK1-dependent autophagy control, and arginine sensing—are coordinated within a single protein and switched between contexts remains unresolved.
  • No unified structural/regulatory model linking the BNB domain, Ser31 phosphorylation, Q167 arginine binding, and condensate assembly
  • Determinants selecting ubiquitin-dependent rescue versus ubiquitin-independent 20S routing per client not defined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 5 GO:0044183 protein folding chaperone 2 GO:0140096 catalytic activity, acting on a protein 2 GO:0140313 molecular sequestering activity 2 GO:0140299 molecular sensor activity 1
Localization
GO:0005783 endoplasmic reticulum 2 GO:0005829 cytosol 2 GO:0005856 cytoskeleton 2 GO:0005634 nucleus 1
Pathway
R-HSA-392499 Metabolism of proteins 4 R-HSA-9612973 Autophagy 4 R-HSA-5357801 Programmed Cell Death 2 R-HSA-162582 Signal Transduction 1 R-HSA-168256 Immune System 1
Partners
AMBRA1HSPA1AHSPA8PINK1SAMD4BSTING1STUB1WDR62
Complex memberships
BAG2 stress-induced microtubule condensate (with HSP70/PA28)BAG2-Hsc70-CHIP ternary complexHsc70-SGTA-Hsp105 extraction complexULK1 kinase complex (effector)

Evidence

Reading pass · 26 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 HeLa cells and acts as an inhibitor of CHIP ubiquitin ligase activity by abrogating CHIP/E2 (UbcH5a) cooperation, thereby inhibiting ubiquitination of chaperone-presented client proteins such as misfolded CFTR and stimulating chaperone-assisted maturation of CFTR. Peptide mass fingerprinting of CHIP complexes, in vitro and in vivo ubiquitylation assays, binding assays Molecular biology of the cell High 16169850 16207813
2005 BAG2 associates with CHIP as part of a ternary complex with Hsc70, and inhibition of CHIP-dependent ubiquitin ligase activity by BAG2 is facilitated in part by ATP-dependent remodeling of the BAG2-Hsc70-CHIP heterocomplex. Co-immunoprecipitation, binding assays, in vitro and in vivo ubiquitylation assays The Journal of biological chemistry High 16169850 16207813
2008 BAG2 contains a structurally novel Hsp70 nucleotide-exchange factor (NEF) domain called the 'brand new bag' (BNB) domain, which forms a dimer. A flanking linker helix and loop bind to Hsc70 to promote ADP-ATP nucleotide exchange. NMR analysis shows that client binding sites and Hsc70-interaction sites of BNB overlap, and Hsc70 can displace clients from BAG2-BNB, indicating a distinct mechanism for regulating Hsp70-mediated protein folding. X-ray crystallography (free and Hsc70-bound structures), NMR analysis, functional nucleotide exchange assays Nature structural & molecular biology High 19029896
2009 The BAG2/Hsp70 complex is tethered to the microtubule and can capture and deliver Tau (preferentially Sarkosyl-insoluble and phosphorylated forms) to the proteasome for ubiquitin-independent degradation. Cellular localization studies, knockdown experiments, tau degradation assays in neurons The Journal of neuroscience Medium 19228967
2013 BAG2 directly binds PINK1 and stabilizes it by decreasing its ubiquitination, thereby preventing proteasome-dependent degradation of PINK1. BAG2 also binds the pathogenic R492X PINK1 mutant more tightly and stabilizes it to a greater extent than wild-type PINK1. Co-immunoprecipitation, ubiquitination assays, western blotting Biochemical and biophysical research communications Medium 24383081
2015 BAG2 inhibits PINK1 degradation by blocking the ubiquitination pathway, thereby stabilizing PINK1 on the outer membrane of depolarized mitochondria and triggering PARKIN-mediated mitophagy; BAG2 acts as an upstream regulator of the PINK1/PARKIN signaling pathway and protects neurons against MPP+-induced oxidative stress. Cell-based ubiquitination assays, mitophagy assays, neuronal viability assays, BAG2 overexpression/knockdown The Journal of biological chemistry Medium 26538564
2015 BAG2 binds to mutant p53 (mutp53) and translocates with it to the nucleus, where it inhibits the MDM2-mutp53 interaction and thereby blocks MDM2-mediated ubiquitination and degradation of mutp53, promoting mutp53 accumulation and gain-of-function in tumor growth, metastasis, and chemoresistance. Co-immunoprecipitation, ubiquitination assays, nuclear fractionation, tumor xenograft assays eLife High 26271008
2016 BAG2 interferes with CHIP-mediated ubiquitination of HSP72 (Hsp70), preventing its degradation. In human primary fibroblasts, BAG2 functionally counteracts increased CHIP levels during aging by inhibiting HSP72 ubiquitination. Co-immunoprecipitation, ubiquitination assays, primary fibroblast cultures from young and aged donors International journal of molecular sciences Medium 28042827
2016 The BAG2-HSC70 chaperone complex regulates the localization of LRK-1 (LRRK2 C. elegans homolog) to the Golgi apparatus, controlling polarized sorting of synaptic vesicle proteins to axons. In unc-23 (BAG2 homolog) mutants, synaptic vesicle proteins mislocalize to both axons and dendrites, phenocopying lrk-1 deletion. hsp-1 mutations suppress the unc-23 but not the lrk-1 defect, placing UNC-23 upstream of or parallel to HSP-1 in LRK-1 Golgi localization. Genetic epistasis in C. elegans (unc-23, hsp-1, lrk-1 mutants), fluorescence microscopy of synaptic vesicle protein localization, Co-IP of human BAG2/HSC70 with LRRK2 Genes to cells Medium 26853528
2017 BAG2 interacts with the propeptide region of pro-cathepsin B, blocking its auto-cleavage processing into mature cathepsin B. BAG2 also regulates pro-cathepsin B/annexin II complex formation and facilitates trafficking of pro-cathepsin-B-containing TGN38-positive vesicles toward the cell periphery, promoting secretion of pro-cathepsin B and leading to metastasis in triple-negative breast cancer. Co-immunoprecipitation, vesicle trafficking assays, BAG2 silencing with tumorigenesis/metastasis readouts, fluorescence microscopy Cell reports Medium 29212038
2018 BAG2 acts as a nucleotide exchange factor (NEF) for Hsc70 and is a component of the cytosolic Hsc70-SGTA-Hsp105 extraction complex; BAG2 stimulates SV40 virus release from Hsc70 to enable virus arrival at the cytosol after ER membrane penetration, promoting infection. Virus infection assays, BAG2 knockdown/depletion, biochemical fractionation, rescue experiments Journal of virology Medium 29769335
2019 BAG2 overexpression in M. tuberculosis-infected macrophages enhances autophagic flux, activates reticulophagy (ER-targeted autophagy), and recruits SQSTM1/p62 to the ER. BAG2-activated autophagy is mediated by MAPK/ERK-driven dissociation of BECN1 from BCL2. The transcription factor XBP1, downstream of ERN1/IRE1 signaling, binds the BAG2 promoter and transcriptionally inhibits BAG2 expression. Overexpression/knockdown assays, autophagic flux assays, immunofluorescence, ChIP of XBP1 on BAG2 promoter, pharmacological inhibitors Autophagy Medium 31711362
2020 LOXL1 interacts with BAG2 via a hydrogen bond between LOXL1-D515 and BAG2-K186, and the lysyl oxidase activity of LOXL1 prevents BAG2 degradation by competing with K186 ubiquitylation, thereby stabilizing BAG2 and promoting glioma cell survival. Co-immunoprecipitation, ubiquitination assays, structural interaction mapping, gain/loss-of-function in cells and animals Cell death and differentiation Medium 32424143
2020 BAG2 binds to ERK1/2 and promotes proliferation and metastasis of gastric cancer cells through ERK1/2 signaling, as shown by immunoprecipitation and functional knockdown assays. Co-immunoprecipitation, BAG2 knockdown, proteomic analysis, cell proliferation/invasion/migration assays Frontiers in oncology Low 32082999
2021 BAG2 inhibits CHIP-mediated ubiquitination and degradation of ERβ in human endometrial stromal cells, thereby stabilizing ERβ protein via the ubiquitin-proteasome pathway. Knockdown of BAG2 and MDM2 together alleviated endometriosis development in mice. HA/FLAG-immunoprecipitation assays, immunoblotting with anti-ubiquitin antibody, murine endometriosis model, cell-based ubiquitination assays Frontiers in cell and developmental biology Medium 33987175
2022 USP49 deubiquitinates and stabilizes BAG2 protein levels, acting downstream of transcriptional activation by c-MYC (c-MYC-USP49-BAG2 axis), thereby promoting colorectal cancer cell proliferation and chemoresistance. Knockdown experiments, ubiquitination assays, Co-immunoprecipitation, cell proliferation/colony formation assays Biochemical and biophysical research communications Medium 35367823
2022 BAG2 marks a distinct phase-separated membraneless organelle (condensate/granule) triggered by stress (particularly hyper-osmotic stress). These BAG2-containing granules lack RNA and ubiquitin, promote client protein degradation via the 20S proteasome in a ubiquitin-independent manner, and contain HSP-70 and PA28 (PSME) family members. On the microtubule, these condensates can traffic to Tau protein. When the proteasome is inhibited, BAG2 condensates traffic to aggresome-like structures. Live-cell fluorescence microscopy, phase separation assays, proteasome inhibition, immunostaining, biochemical fractionation Nature communications High 35654899
2023 BAG2 localizes within mutant p53 aggregates, interacts with misfolded p53 mutants, exacerbates formation of mutant p53 aggregates, and recruits HSP90 to promote propagation and maintenance of these aggregates. BAG2-mediated mutant p53 aggregation inhibits the mitochondrial apoptosis pathway, leading to chemoresistance. Co-immunoprecipitation, immunofluorescence, semi-denaturing detergent-agarose gel electrophoresis, BAG2 silencing, tumor models Theranostics Medium 36593950
2024 BAG2 is an effector of the ULK1 kinase complex. In growth conditions, unphosphorylated BAG2 sequesters AMBRA1 (a VPS34 complex member), attenuating autophagy. During starvation, ULK1 phosphorylates BAG2 on Ser31, releasing AMBRA1 and supporting its recruitment to the ER membrane to positively regulate autophagy initiation. Affinity purification and proximity labeling mass spectrometry, ULK1 kinase assays, site-directed mutagenesis of Ser31, AMBRA1 localization assays, autophagy flux assays Cell reports High 39207901
2024 DNAJ-PKAc fusion kinase (fibrolamellar carcinoma) phosphorylates BAG2, which is recruited to the fusion kinase via Hsp70 association. The DNAJ-PKAc/Hsp70/BAG2 axis promotes chemoresistance in fibrolamellar carcinoma cells. Proximity proteomics, biochemical analyses, live-cell photoactivation microscopy, kinase substrate assays, drug studies Cell reports Medium 38236773
2025 BAG2 acts as an intracellular arginine sensor that directly binds arginine at glutamine residue Q167. Upon arginine deficiency, BAG2 releases SAMD4B, leading to β-catenin degradation and ATF4 stabilization to enhance cell survival. When arginine is abundant, strengthened BAG2-SAMD4B binding prevents β-catenin degradation and activates the Wnt/β-catenin pathway to support cell growth. Unbiased screening in human cancer cell lines, biochemical binding assays, site-directed mutagenesis of Q167, co-immunoprecipitation, cellular signaling readouts Molecular cell High 40555234
2025 BAG2 inhibits STUB1/CHIP-mediated K48-linked ubiquitination of STING at residues K338 and K370 by forming a complex with STUB1, thereby stabilizing STING protein and activating the type I interferon pathway to suppress cervical cancer progression. Co-immunoprecipitation, site-directed mutagenesis (K338/K370), ubiquitination assays, BAG2 overexpression/knockdown, interferon signaling readouts Advanced science Medium 40364789
2025 BAG2 interacts directly with the microcephaly protein WDR62. Under stress, both proteins re-localize to cytoplasmic granules. In WDR62-deficient cells, elevated BAG2 levels destabilize the purine salvage enzyme HPRT; BAG2 knockdown in WDR62-deficient cells restores HPRT levels. Microcephaly-associated WDR62 mutations disrupt interaction with BAG2 and fail to restore HPRT levels. Co-immunoprecipitation, BAG2 knockdown, HPRT stability assays, purinosome imaging, WDR62 mutant rescue assays The EMBO journal Medium 41787126
2025 BAG2 inhibits the ubiquitination degradation of HSP70 by interacting with CHIP, thereby increasing HSP70-Apaf1 binding and reducing mitochondrial cytochrome C release, which inhibits apoptosome assembly and suppresses mitochondrial apoptosis in gastric cancer cells. Co-immunoprecipitation, ubiquitination assays, apoptosis assays (cytochrome C release, caspase activation), BAG2 overexpression/knockdown Frontiers in immunology Medium 40755756
2024 BAG2 maintains mitophagy activation by binding to PINK1 and protecting it from proteasome-dependent degradation. Bag2 overexpression preserves mitochondrial function and protects against doxorubicin-induced cardiotoxicity. Co-immunoprecipitation, proteasome inhibition assays, mitophagy assays, in vitro and in vivo (mouse) models of doxorubicin cardiotoxicity Toxicology Medium 39442788
2014 BAG2 directly binds pathogenic ataxin3-80Q and inhibits its ubiquitination, stabilizing the polyglutamine-expanded protein. Co-immunoprecipitation, ubiquitination assays, co-immunofluorescence The International journal of neuroscience Low 25006867

Source papers

Stage 0 corpus · 54 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 139 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 84 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 55 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
2013 Curcumin-induced upregulation of the anti-tau cochaperone BAG2 in primary rat cortical neurons. Neuroscience letters 47 24035895
2017 Co-chaperone BAG2 Determines the Pro-oncogenic Role of Cathepsin B in Triple-Negative Breast Cancer Cells. Cell reports 46 29212038
2022 Stress routes clients to the proteasome via a BAG2 ubiquitin-independent degradation condensate. Nature communications 44 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 Identification of BAG2 and Cathepsin D as Plasma Biomarkers for Parkinson's Disease. Clinical and translational science 30 33202088
2020 BAG2 Promotes Proliferation and Metastasis of Gastric Cancer via ERK1/2 Signaling and Partially Regulated by miR186. Frontiers in oncology 29 32082999
2023 BAG2 drives chemoresistance of breast cancer by exacerbating mutant p53 aggregate. Theranostics 27 36593950
2022 c-MYC-USP49-BAG2 axis promotes proliferation and chemoresistance of colorectal cancer cells in vitro. Biochemical and biophysical research communications 25 35367823
2018 Bag2 Is a Component of a Cytosolic Extraction Machinery That Promotes Membrane Penetration of a Nonenveloped Virus. Journal of virology 24 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
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 18 33987175
2016 BAG2 Interferes with CHIP-Mediated Ubiquitination of HSP72. International journal of molecular sciences 18 28042827
2023 GNB1 promotes hepatocellular carcinoma progression by targeting BAG2 to activate P38/MAPK signaling. Cancer science 15 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 15 26496817
2024 The ULK1 effector BAG2 regulates autophagy initiation by modulating AMBRA1 localization. Cell reports 14 39207901
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
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
2025 BAG2 releases SAMD4B upon sensing of arginine deficiency to promote tumor cell survival. Molecular cell 9 40555234
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
2022 BAG2 prevents Tau hyperphosphorylation and increases p62/SQSTM1 in cell models of neurodegeneration. Molecular biology reports 9 35612780
2018 The role of Bag2 in neurotoxicity induced by the anesthetic sevoflurane. Journal of cellular biochemistry 9 30548665
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
2025 BAG2 Inhibits Cervical Cancer Progression by Modulating Type I Interferon Signaling through Stabilizing STING. Advanced science (Weinheim, Baden-Wurttemberg, Germany) 6 40364789
2021 BAG2 mediates coelomocyte apoptosis in Vibrio splendidus challenged sea cucumber Apostichopus japonicus. International journal of biological macromolecules 6 34418417
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
2025 Disruption of Hsp70.14-BAG2 Protein-Protein interactions using deep Learning-Driven peptide design and molecular simulations. Computers in biology and medicine 3 40466244
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
2026 BAG2 Condensates Couple Proteostasis to CD8+T Cell Surveillance. bioRxiv : the preprint server for biology 0 42094418
2026 In vivo analysis of UNC-23 reveals residues critical for BAG2 domain function. bioRxiv : the preprint server for biology 0 42244563
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

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