Affinage

HSPBP1

Hsp70-binding protein 1 · UniProt Q9NZL4

Length
359 aa
Mass
39.3 kDa
Annotated
2026-06-10
35 papers in source corpus 20 papers cited in narrative 20 extracted findings
Cross-family judge vs UniProt: tie faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

HSPBP1 (yeast ortholog Fes1) is an armadillo-repeat nucleotide exchange factor for Hsp70/Hsc70 that couples chaperone cycling to protein quality control (PMID:12417338, PMID:15694338). Structurally it pairs a helical armadillo domain II, whose concave face embraces lobe II of the Hsp70 ATPase domain and sterically displaces lobe I to lower nucleotide affinity, with a flexible N-terminal release domain that mimics substrate and competes for the Hsp70 substrate-binding domain, so that nucleotide exchange and active eviction of persistent clients occur together (PMID:15694338, PMID:29323280, PMID:12651857). Through this triaging activity HSPBP1 selectively releases misfolded proteins from Hsp70 and routes them toward polyubiquitylation and proteasomal degradation; loss of the factor causes substrate aggregation and a heightened heat-shock response, and a dedicated cytosolic isoform (Fes1S) is required for this degradative function (PMID:23530227, PMID:26912797). In parallel, when complexed with Hsc70 HSPBP1 inhibits the CHIP ubiquitin ligase, stabilizing selected clients including immature CFTR and the inducible chaperones HSPA1L and HSPA2 in testes, where its loss in mice causes meiotic failure and spermatocyte apoptosis (PMID:15215316, PMID:24899640). By the same CHIP-suppressing mechanism HSPBP1 limits clearance of mutant huntingtin in neurons (PMID:28847953). HSPBP1 additionally antagonizes Hsp70 cytoprotection at lysosomes to promote membrane permeabilization and cell death (PMID:17855353), regulates steroid-receptor activity by reducing Hsp70 binding to the receptor ligand-binding domain (PMID:24454860), and is an integral RNA-binding component of oxidative-stress granules where it associates with G3BP1, HuR, and TIA-1/TIAR (PMID:32235396). Its exchange activity is redox-tunable through reversible methionine oxidation of a cluster in the armadillo core, reversed by MsrA/MsrB (PMID:31806703).

Mechanistic history

Synthesis pass · year-by-year structured walk · 20 steps
  1. 2002 High

    Established the core biochemical identity of HspBP1 by showing it is a nucleotide exchange factor that drives nucleotide dissociation from Hsp70-class chaperones, defining a eukaryotic NEF family with yeast Fes1p.

    Evidence In vitro nucleotide dissociation and refolding assays with yeast Ssa1p and mammalian Hsc70

    PMID:12417338

    Open questions at the time
    • Structural basis of exchange not yet resolved
    • Did not address substrate release or downstream fate of clients
  2. 2003 Medium

    Mapped the two-domain architecture, showing the helical domain II suffices to bind Hsp70 and remodel its ATPase domain while the unstructured N-terminal domain enhances both functions.

    Evidence Circular dichroism, limited proteolysis, truncation mutagenesis, and luciferase renaturation assays

    PMID:12651857

    Open questions at the time
    • Molecular role of domain I not defined
    • Single-lab biochemical study without structure
  3. 2003 Medium

    Showed how the inhibitory Hsp70-HspBP1 complex is resolved, requiring cooperative action of Hsp40 and TPR1 rather than either cochaperone alone.

    Evidence In vitro luciferase refolding, Kd competition assays, and inducible Hsp70 cell system

    PMID:14503850

    Open questions at the time
    • Physiological context of TPR1/Hsp40 cooperation untested
    • Single lab
  4. 2004 High

    Identified a degradation-protective branch: when bound to Hsc70, HspBP1 inhibits CHIP ubiquitin ligase activity, sparing immature CFTR from proteasomal destruction and promoting its maturation.

    Evidence Reciprocal Co-IP, in vitro ubiquitin ligase assay, CFTR pulse-chase, and RNAi

    PMID:15215316

    Open questions at the time
    • Selectivity of which clients are protected not defined
    • Reconciliation with the degradative NEF role not addressed
  5. 2005 High

    Provided the atomic mechanism of exchange, showing the armadillo concave face embraces ATPase lobe II and displaces lobe I to reduce nucleotide affinity, a mechanism distinct from BAG-1 and GrpE.

    Evidence X-ray crystallography of HspBP1 alone and with the Hsp70 ATPase domain, plus Fes1p yeast deletion genetics

    PMID:15694338

    Open questions at the time
    • Did not capture substrate release contacts
    • Full-length complex structure not solved
  6. 2007 Medium

    Linked HspBP1 to cell-death decisions, showing it antagonizes Hsp70 stabilization of lysosomal membranes to promote permeabilization, cathepsin release, and caspase activation in a Hsp70-binding-dependent manner.

    Evidence Ectopic expression, RNAi, lysosomal permeability and cathepsin/caspase assays, Hsp70-binding mutant

    PMID:17855353

    Open questions at the time
    • Direct lysosomal localization mechanism unclear
    • Single lab
  7. 2009 Medium

    Extended HspBP1 to extracellular signaling, showing secreted HspBP1 augments Hsp72-driven EGFR phosphorylation and ERK1/2 activation via its N-terminal domain.

    Evidence Co-IP from conditioned medium, EGFR/ERK signaling assays, N-terminal deletion analysis

    PMID:18986301

    Open questions at the time
    • Receptor for the extracellular complex unidentified
    • Physiological relevance of secretion unclear
  8. 2011 Medium

    Showed HspBP1 binds Tag7 (PGRP-S) and Hsp70 to neutralize the cytotoxic Tag7-Hsp70 complex and lower the ATP needed for its dissociation.

    Evidence Co-IP, cytotoxicity and ATP-dependent dissociation assays in CD8+ lymphocytes

    PMID:21247889

    Open questions at the time
    • Structural basis of Tag7 binding unknown
    • Single lab
  9. 2013 High

    Defined the triaging role, showing Fes1 selectively engages Hsp70-bound misfolded clients and triggers their release for polyubiquitylation; its loss causes aggregation and a strong stress response.

    Evidence FES1 deletion yeast genetics with polyubiquitylation, aggregation, and heat-shock reporter assays

    PMID:23530227

    Open questions at the time
    • Molecular contacts driving release not yet resolved (addressed in 2018)
    • Coupling to specific E3 ligases not defined
  10. 2014 High

    Provided in vivo physiological context for CHIP inhibition, showing HSPBP1 stabilizes HSPA1L and HSPA2 in testes and is required for meiosis and spermatocyte survival.

    Evidence HSPBP1 knockout mice, Western blot, ubiquitylation assays, synaptonemal complex immunofluorescence

    PMID:24899640

    Open questions at the time
    • Tissue-specific basis of client selection not defined
    • Relationship to the degradative NEF function unresolved
  11. 2014 Medium

    Identified a steroid-receptor regulatory role, showing HspBP1 reduces Hsp70 binding to the GR ligand-binding domain and inhibits GR/MR/AR transcriptional activity, unlike BAG-1M.

    Evidence Co-IP, pulldown, and GR/MR/AR reporter assays with overexpression

    PMID:24454860

    Open questions at the time
    • Mechanism of receptor LBD effect not deeply dissected
    • Endogenous relevance untested
  12. 2016 High

    Revealed isoform-specific compartmentalization, defining a nuclear Fes1L and cytosolic Fes1S, with only Fes1S supporting proteasomal degradation of misfolded proteins.

    Evidence RNA-seq, isoform constructs, fluorescence localization, isoform-specific yeast deletions, degradation and heat-shock assays

    PMID:26912797

    Open questions at the time
    • Function of nuclear Fes1L not defined
    • Human HSPBP1 isoform equivalence not established
  13. 2017 High

    Demonstrated disease-relevant CHIP suppression in brain, showing abundant neuronal HspBP1 dampens CHIP activity and its silencing reduces mutant huntingtin aggregation and neuropathology.

    Evidence CRISPR-Cas9 knockdown, CHIP ligase assays, Co-IP, and HD knock-in mouse model

    PMID:28847953

    Open questions at the time
    • Whether HspBP1 lowering is broadly protective across proteinopathies unknown
    • Effect on global proteostasis in neurons not assessed
  14. 2018 High

    Resolved the substrate-release mechanism, showing a flexible N-terminal release domain mimics substrate and competes at the Hsp70 substrate-binding domain, distinct from armadillo-driven nucleotide exchange.

    Evidence In vitro peptide competition, release-domain mutagenesis, yeast and mammalian complementation, structural analysis of the RD

    PMID:29323280

    Open questions at the time
    • Kinetic coupling of exchange and release not fully quantified
    • Client-specificity determinants of the RD unclear
  15. 2019 High

    Established redox regulation, showing reversible methionine oxidation of an armadillo-core cluster inhibits NEF activity, reversed by Mxr1/Mxr2 (MsrA/MsrB).

    Evidence In vitro and in-cell oxidation/activity assays, site-directed mutagenesis, and reductase genetics in yeast

    PMID:31806703

    Open questions at the time
    • Physiological oxidative conditions triggering this in cells not defined
    • Conservation of the methionine cluster in human HSPBP1 not tested
  16. 2019 Medium

    Uncovered Hsp70-independent activities, showing Fes1 mutants unable to bind Hsp70 still support Vid-pathway degradation and CWI signaling by directly binding Fbp1 and capturing the kinase Slt2.

    Evidence Hsp70-interaction-defective mutants, in vitro Fbp1 binding, Slt2 pulldown, and yeast growth/Vid assays

    PMID:31242183

    Open questions at the time
    • Mammalian equivalents of these moonlighting functions unknown
    • Single lab in yeast
  17. 2020 Medium

    Assigned a stress-granule and RNA-binding role, showing HspBP1 is an integral SG component that binds polyA-RNA and RNA homopolymers and regulates SG assembly.

    Evidence Immunofluorescence, Co-IP/MS, in vitro RNA binding, siRNA, and overexpression with single-granule analysis

    PMID:32235396

    Open questions at the time
    • RNA-binding region not mapped
    • Relationship between SG role and NEF activity unresolved
  18. 2021 Medium

    Linked HspBP1 to innate immunity, showing it stabilizes RIG-I by inhibiting K48-linked ubiquitination, enhancing IRF3 activation and IFN-beta production.

    Evidence Overexpression, siRNA, CRISPR knockout, K48-specific ubiquitination, IRF3 phosphorylation, and IFN-beta reporter assays

    PMID:33713958

    Open questions at the time
    • Direct E3 ligase antagonized not identified
    • Whether CHIP or another ligase is involved unclear
  19. 2022 Medium

    Connected HspBP1 to DNA repair and radioresistance, showing it interacts with BRCA1 to promote homologous recombination and separately inhibits Hsp70-Apaf-1 association to promote survival after irradiation.

    Evidence Co-IP, HR repair assay, xenograft model, siRNA/overexpression, and Apaf-1/Hsp70 co-IP

    PMID:35387978

    Open questions at the time
    • Mechanism by which HspBP1 aids BRCA1 in HR undefined
    • Single lab
  20. 2026 Low

    Identified a druggable cysteine, showing HSPBP1 Cys201 is covalently targeted by parthenolide and contributes to necroptosis inhibition.

    Evidence Mass spectrometry adduct mapping, purified-protein co-incubation, siRNA, necroptosis assay, and mouse AAA model

    PMID:42014672

    Open questions at the time
    • Mechanism downstream of Cys201 modification not dissected
    • Single study without independent confirmation

Open questions

Synthesis pass · forward-looking unresolved questions
  • How HSPBP1 reconciles its dual outputs — actively releasing clients for degradation versus protecting clients by inhibiting CHIP — and what determines client triage between these fates remains unresolved.
  • No defined switch governing degradative versus protective branches
  • Human full-length HSPBP1-Hsp70-client complex structure unsolved
  • Client-selection rules across tissues unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 3 GO:0140096 catalytic activity, acting on a protein 3 GO:0008092 cytoskeletal protein binding 2 GO:0003723 RNA binding 1
Localization
GO:0005576 extracellular region 1 GO:0005634 nucleus 1 GO:0005829 cytosol 1
Pathway
R-HSA-392499 Metabolism of proteins 3 R-HSA-8953897 Cellular responses to stimuli 3 R-HSA-5357801 Programmed Cell Death 2 R-HSA-168256 Immune System 1
Partners
BRCA1EGFRG3BP1HSPA1LHSPA2HSPA8PGLYRP1STUB1
Complex memberships
stress granule

Evidence

Reading pass · 20 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2005 Crystal structure of HspBP1 alone and in complex with the Hsp70 ATPase domain reveals an armadillo-repeat fold whose concave face embraces lobe II of the ATPase domain; steric conflict displaces lobe I, reducing nucleotide affinity — a mechanism distinct from BAG-1 or GrpE, which instead trigger a conformational change in lobe II. X-ray crystallography (crystal structure of HspBP1 alone and in complex with Hsp70 ATPase domain fragment); yeast genetics (Fes1p deletion showing requirement for protein folding at 37°C) Molecular cell High 15694338
2002 HspBP1 is a nucleotide exchange factor (NEF) for Hsc70; it promotes nucleotide dissociation from both yeast Ssa1p and mammalian Hsc70 in vitro, establishing it as a member of the eukaryotic NEF family homologous to yeast Fes1p. In vitro nucleotide dissociation assay; chaperone-mediated protein refolding assay FEBS letters High 12417338
2004 HspBP1 inhibits the ubiquitin ligase activity of CHIP when HspBP1 is complexed with Hsc70, thereby interfering with CHIP-induced proteasomal degradation of immature CFTR and stimulating CFTR maturation. Co-immunoprecipitation; ubiquitin ligase activity assay; pulse-chase analysis of CFTR maturation; RNAi knockdown Molecular biology of the cell High 15215316
2003 HspBP1 has two structural domains: an N-terminal largely unstructured domain I (aa 1–83) and a helical domain II (aa 84–359). Domain II is sufficient to bind Hsp70 and alter the conformation of the Hsp70 ATPase domain; domain I enhances both functions. Circular dichroism; limited proteolysis; truncation mutagenesis; Hsp70-binding assay in reticulocyte lysate; luciferase renaturation assay The Journal of biological chemistry Medium 12651857
2013 Yeast Fes1 (ortholog of HspBP1) acts as a cytosolic triaging factor that selectively interacts with misfolded proteins bound to Hsp70 and triggers their release; in the absence of Fes1, misfolded proteins fail to undergo polyubiquitylation, aggregate, and induce a strong heat-shock response. Yeast genetics (FES1 deletion); polyubiquitylation assay; protein aggregation analysis; heat-shock reporter assay; binding assays with misfolded substrates Proceedings of the National Academy of Sciences of the United States of America High 23530227
2018 Fes1 and HspBP1 each contain a flexible N-terminal release domain (RD) with substrate-mimicking properties; the RD contacts the Hsp70 substrate-binding domain and competes with peptide substrate for binding, ensuring efficient release of persistent substrates. The armadillo domain triggers nucleotide exchange while the RD drives substrate release. In vitro peptide competition assays; mutagenesis of the release domain; yeast complementation; mammalian cell functional assays; NMR/structural analysis of RD Nature structural & molecular biology High 29323280
2016 The FES1 transcript is alternatively spliced at its 3' end to produce two isoforms: Fes1L (targeted to the nucleus, the first identified nuclear Hsp70 NEF) and Fes1S (cytosolic). Fes1S is essential for proteasomal degradation of misfolded proteins and proteostasis; Fes1L localizes to the nucleus but cannot substitute for cytosolic Fes1S function. RNA-seq; isoform-specific expression constructs; fluorescence microscopy for localization; yeast genetics (isoform-specific deletions); ubiquitin-proteasome degradation assays; heat-shock reporter assay Molecular biology of the cell High 26912797
2014 HSPBP1 inhibits CHIP-mediated ubiquitylation and proteasomal degradation of inducible HSP70 family members (HSPA1L and HSPA2) in testes, thereby stabilizing these chaperones at the posttranslational level. Loss of HSPBP1 in mice leads to impaired meiosis and spermatocyte apoptosis due to reduced HSPA1L and HSPA2 levels. HSPBP1 knockout mice; Western blot analysis; ubiquitylation assays; meiotic phenotype analysis (immunofluorescence of synaptonemal complexes) Molecular biology of the cell High 24899640
2017 Neurons express abundant HspBP1 which suppresses CHIP ubiquitin ligase activity, resulting in low CHIP-mediated degradation of misfolded proteins. CRISPR-Cas9 silencing of HspBP1 in neurons increased CHIP activity and reduced mutant huntingtin aggregation and neuropathology in HD knock-in mice. CRISPR-Cas9 knockdown; CHIP ubiquitin ligase activity assay; Co-immunoprecipitation; immunofluorescence; Western blot; HD knock-in mouse model Proceedings of the National Academy of Sciences of the United States of America High 28847953
2003 The inhibitory effect of HspBP1 on Hsp70-dependent protein folding can be reversed by the cooperative action of both Hsp40 and TPR1 together; neither cochaperone alone is sufficient to dissociate the Hsp70-HspBP1 complex. In vitro luciferase refolding assay; Kd measurement by competition assays; Hela cell tetracycline-inducible Hsp70 expression system Molecules and cells Medium 14503850
2019 Fes1 undergoes reversible methionine oxidation at a cluster of three methionine residues in its core armadillo domain under oxidizing conditions; this oxidation inhibits NEF activity and consequently alters Hsp70 chaperone activity. Oxidation is reversed by cytoplasmic methionine sulfoxide reductases Mxr1 (MsrA) and Mxr2 (MsrB). In vitro oxidation and activity assays with recombinant proteins; site-directed mutagenesis; in-cell oxidation assays; genetic manipulation of Mxr1/Mxr2 The Journal of biological chemistry High 31806703
2007 HspBP1 antagonizes the prosurvival function of Hsp70 by interfering with Hsp70-mediated stabilization of lysosomal membranes; ectopic HspBP1 promotes lysosomal membrane permeabilization, cathepsin release into cytosol, and caspase-3 activation in response to anticancer drugs, in a manner dependent on its ability to bind Hsp70. Ectopic expression; RNAi knockdown; lysosomal membrane permeability assay; cathepsin release assay; caspase-3 activation assay; Hsp70-binding mutant analysis The Journal of biological chemistry Medium 17855353
2011 HspBP1 binds directly to Tag7 (PGRP-S) as well as to Hsp70, thereby eliminating the cytotoxic activity of the Tag7-Hsp70 complex and lowering the ATP concentration required to dissociate Tag7 from the Hsp70 peptide-binding site. Co-immunoprecipitation; cytotoxicity assays; ATP-dependent dissociation assay; immunodetection in CD8+ lymphocytes The Journal of biological chemistry Medium 21247889
2009 Extracellular HspBP1 co-immunoprecipitates with extracellular Hsp72 in conditioned medium and synergistically augments Hsp72-mediated EGFR phosphorylation and downstream ERK1/2 activation; the N-terminal domain of HspBP1 is required for this activity. Co-immunoprecipitation from conditioned medium; EGFR phosphorylation assay; ERK1/2 activation assay; N-terminal deletion mutant analysis; chromogranin A co-localization Biology of the cell Medium 18986301
2020 HspBP1 is an integral component of cytoplasmic stress granules (SGs) under oxidative stress, co-localizing with G3BP1, HuR, and TIA-1/TIAR; HspBP1 associates with polyA-RNA in vivo and binds RNA homopolymers directly in vitro. HspBP1 knockdown impairs SG assembly while overexpression promotes SG formation without stress, with the Hsp70-binding domain contributing to SG regulation. Immunofluorescence microscopy; co-immunoprecipitation; mass spectrometry; in vitro RNA binding assay; siRNA knockdown; overexpression; single-granule analysis Cells Medium 32235396
2014 HspBP1 reduces Hsp70 binding to the GR ligand-binding domain and inhibits glucocorticoid, mineralocorticoid, and androgen receptor transcriptional activity, in contrast to BAG-1M which has dose-dependent stimulatory/inhibitory effects. Hsp40 and steroid receptors preferentially associate with BAG-1M rather than HspBP1 in pulldown assays. Co-immunoprecipitation; pulldown assays; reporter gene assays (GR, MR, AR activity); overexpression PloS one Medium 24454860
2021 HSPBP1 promotes RIG-I-mediated antiviral signaling by inhibiting K48-linked ubiquitination of RIG-I, thereby stabilizing RIG-I protein and enhancing IRF3 activation and IFN-β production upon Sendai virus infection. Overexpression; siRNA knockdown; CRISPR knockout; ubiquitination assay (K48-specific); IRF3 phosphorylation assay; IFN-β reporter assay Molecular immunology Medium 33713958
2022 HspBP1 interacts with BRCA1 and promotes BRCA1-mediated homologous recombination DNA repair; HspBP1 knockdown or overexpression in BRCA1-proficient breast cancer cells reduces HR repair efficiency and alters tumorigenicity. Independently, HspBP1 inhibits the association of Hsp70 with Apaf-1 to promote cell survival after ionizing radiation, regardless of BRCA1 status. Co-immunoprecipitation (HspBP1-BRCA1 interaction); HR repair assay; xenograft tumor model; siRNA knockdown; overexpression; Apaf-1/Hsp70 co-IP Cell death & disease Medium 35387978
2019 Yeast Fes1 has Hsp70-independent roles: Fes1 mutants defective for Hsp70 interaction retain the ability to support vacuole import and degradation (Vid pathway) degradation of gluconeogenic enzymes and cell wall integrity (CWI) signaling. Fes1 binds directly to the Vid substrate Fbp1 in vitro and captures the CWI kinase Slt2 from cell lysates via its armadillo domain. Hsp70-interaction-defective Fes1 mutants; in vitro binding assay (Fes1 + Fbp1); pulldown of Slt2 from lysate; yeast growth assays; Vid pathway assay PLoS genetics Medium 31242183
2026 HSPBP1 Cys201 is identified as a target of the anti-necroptotic compound parthenolide (PTL); covalent modification at Cys201 contributes to necroptosis inhibition, and HSPBP1 knockdown confers partial resistance to necroptosis. Mass spectrometry (PTL-HSPBP1 covalent adduct at Cys201); co-incubation with purified HSPBP1; siRNA knockdown; necroptosis assay in HT-29 cells; mouse AAA model Cell death & disease Low 42014672

Source papers

Stage 0 corpus · 35 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2005 Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange. Molecular cell 165 15694338
2004 The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator. Molecular biology of the cell 139 15215316
2002 HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factor. FEBS letters 81 12417338
2013 Hsp70 nucleotide exchange factor Fes1 is essential for ubiquitin-dependent degradation of misfolded cytosolic proteins. Proceedings of the National Academy of Sciences of the United States of America 68 23530227
2015 GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG domain proteins: nucleotide exchange factors for Hsp70 molecular chaperones. Sub-cellular biochemistry 48 25487014
2018 Nucleotide exchange factors Fes1 and HspBP1 mimic substrate to release misfolded proteins from Hsp70. Nature structural & molecular biology 45 29323280
2017 Differential HspBP1 expression accounts for the greater vulnerability of neurons than astrocytes to misfolded proteins. Proceedings of the National Academy of Sciences of the United States of America 43 28847953
2016 Cytosolic splice isoform of Hsp70 nucleotide exchange factor Fes1 is required for the degradation of misfolded proteins in yeast. Molecular biology of the cell 36 26912797
2007 Anticancer drugs up-regulate HspBP1 and thereby antagonize the prosurvival function of Hsp70 in tumor cells. The Journal of biological chemistry 26 17855353
2003 HspBP1, an Hsp70 cochaperone, has two structural domains and is capable of altering the conformation of the Hsp70 ATPase domain. The Journal of biological chemistry 26 12651857
2014 HSP70-binding protein HSPBP1 regulates chaperone expression at a posttranslational level and is essential for spermatogenesis. Molecular biology of the cell 24 24899640
2003 Increased expression of the Hsp70 cochaperone HspBP1 in tumors. Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine 23 15004487
2014 Hsp70 cochaperones HspBP1 and BAG-1M differentially regulate steroid hormone receptor function. PloS one 22 24454860
2011 The heat shock-binding protein (HspBP1) protects cells against the cytotoxic action of the Tag7-Hsp70 complex. The Journal of biological chemistry 19 21247889
2019 Activity of the yeast cytoplasmic Hsp70 nucleotide-exchange factor Fes1 is regulated by reversible methionine oxidation. The Journal of biological chemistry 18 31806703
2020 The Co-Chaperone HspBP1 Is a Novel Component of Stress Granules that Regulates Their Formation. Cells 17 32235396
2008 HspBP1 levels are elevated in breast tumor tissue and inversely related to tumor aggressiveness. Cell stress & chaperones 17 18987994
2003 Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses Hsp70-HspBp1 complex formation. Molecules and cells 17 14503850
2023 Nucleotide Exchange Factors for Hsp70 Molecular Chaperones: GrpE, Hsp110/Grp170, HspBP1/Sil1, and BAG Domain Proteins. Sub-cellular biochemistry 16 36520302
2022 HspBP1 is a dual function regulatory protein that controls both DNA repair and apoptosis in breast cancer cells. Cell death & disease 13 35387978
2009 Extracellular HspBP1 and Hsp72 synergistically activate epidermal growth factor receptor. Biology of the cell 12 18986301
2012 Effect of exercise on the expression of HSPBP1, PGLYRP1, and HSPA1A genes in human leukocytes. Bulletin of experimental biology and medicine 11 23113305
2005 Development of a sensitive assay for the measurement of antibodies against heat shock protein binding protein 1 (HspBP1): increased levels of anti-HspBP1 IgG are prevalent in HIV infected subjects. Journal of medical virology 11 15977250
2019 Hsp70-nucleotide exchange factor (NEF) Fes1 has non-NEF roles in degradation of gluconeogenic enzymes and cell wall integrity. PLoS genetics 9 31242183
2006 Expression of the cochaperone HspBP1 is not coordinately regulated with Hsp70 expression. Cell biology international 8 16677834
2022 Identification of 5' upstream sequence involved in HSPBP1 gene transcription and its downregulation during HIV-1 infection. Virus research 5 36581045
2021 HSPBP1 facilitates cellular RLR-mediated antiviral response by inhibiting the K48-linked ubiquitination of RIG-I. Molecular immunology 5 33713958
2015 Quantitative analysis of the interplay between hsc70 and its co-chaperone HspBP1. PeerJ 4 26713263
2011 Extracellular HspBP1 inhibits formation of a cytotoxic Tag7-Hsp70 complex in vitro and in human serum. Biochimie 4 22037021
2010 Long-term exercises increase the concentration of HspBP1, a co-chaperone of 70-KDa heat shock protein. Bulletin of experimental biology and medicine 4 21165407
2000 Isolation and characterization of isoforms of HspBP1, inhibitors of Hsp70. Biochimica et biophysica acta 4 10786638
2020 Heat-stress induced expression of stress-inducible nucleotide exchange factor Fes1 in seagrass Zostera japonica. Ecotoxicology (London, England) 3 32162033
2019 HspBP1 and anti-HspBP1 levels in the serum of HIV-infected individuals are associated to the disease progression. Journal of applied microbiology 3 30786116
2024 HspBP1 in Complex with the Peptide of the Innate Immunity Protein Tag7 is Able to Lyse Tumor Cells Carrying TNFR1 Receptor. Doklady. Biochemistry and biophysics 2 38189890
2026 Identification of human MLKL Cys184 and HSPBP1 Cys201 as novel cellular targets for necroptosis. Cell death & disease 0 42014672

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