Affinage

STUB1

E3 ubiquitin-protein ligase CHIP · UniProt Q9UNE7

Round 2 corrected
Length
303 aa
Mass
34.9 kDa
Annotated
2026-04-28
130 papers in source corpus 37 papers cited in narrative 37 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

STUB1 (CHIP) is a U-box E3 ubiquitin-protein ligase and co-chaperone that functions as a central node in protein quality control, coupling the Hsc70/Hsp70/Hsp90 chaperone machinery to the ubiquitin–proteasome system and selective autophagy to triage misfolded, phosphorylated, or otherwise aberrant client proteins for degradation. Its N-terminal TPR domain docks onto Hsc70/Hsp70 and Hsp90, while its C-terminal U-box domain recruits UbcH5-family E2 enzymes to catalyze K48-linked (degradative) or K63-linked (non-degradative/signaling) polyubiquitination of a broad substrate repertoire—including phosphorylated tau, CFTR, androgen receptor/AR-V7, glucocorticoid receptor, SMAD3, IFNγ-R1/JAK1, IL-4Rα, YAP1, TFEB, BMAL1, AGO2/Dicer, GPX4, METTL14, BCAT1, LATS2, and inhibited 26S proteasomes—thereby governing proteostasis, signal termination (TGF-β, NF-κB, IFNγ, Hippo/YAP, IL-4/STAT6), circadian clock regulation, autophagy–lysosome biogenesis, antiviral RNAi, ferroptosis, and cellular senescence (PMID:10330192, PMID:11557750, PMID:11146632, PMID:17304350, PMID:24251647, PMID:28754656, PMID:32723828, PMID:35395848, PMID:35533808, PMID:38110356). STUB1 preferentially ubiquitinates phosphorylated tau over unmodified tau, suppressing its aggregation and seeding, and this selectivity depends on a phosphorylation-dependent degron recognized by the TPR domain (PMID:37330289, PMID:14962978). STUB1 also regulates proteaphagy by attaching K63-linked ubiquitin chains to inhibited 26S proteasomes, directing them through HDAC6/dynein-dependent aggresome formation to autophagic clearance (PMID:32723828). Biallelic loss-of-function mutations in STUB1 cause autosomal recessive spinocerebellar ataxia (SCAR16), and dominant mutations cause SCA48, consistent with its essential role in neuronal proteostasis (PMID:14962978, PMID:28754656).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 1999 High

    The first mechanistic question was whether Hsc70/Hsp70 chaperones are subject to co-factor regulation beyond classical cochaperones; the identification of CHIP as a TPR-domain protein that binds Hsc70/Hsp70 and inhibits their ATPase-driven refolding cycle established a new class of negative chaperone regulators.

    Evidence Yeast two-hybrid, GST pulldown, co-IP from human skeletal muscle, ATPase and luciferase refolding assays with recombinant proteins

    PMID:10330192

    Open questions at the time
    • No substrate degradation activity was demonstrated
    • Hsp90 interaction not yet tested
    • Physiological relevance in vivo not assessed
  2. 2001 High

    The critical advance was demonstrating that CHIP is not merely a chaperone inhibitor but a bona fide U-box E3 ubiquitin ligase that partners with UbcH5 E2 enzymes to ubiquitinate chaperone-bound misfolded substrates, remodels Hsp90 complexes from folding to degradation mode, and targets client proteins (CFTR, glucocorticoid receptor) for proteasomal destruction—establishing the chaperone-associated ubiquitin ligase paradigm.

    Evidence In vitro ubiquitylation with purified components, U-box deletion mutagenesis, dominant-negative CHIP, Hsp90 complex remodeling assays, proteasome inhibitor rescue in cells

    PMID:11146632 PMID:11146634 PMID:11557750 PMID:11743028

    Open questions at the time
    • Structural basis for U-box/E2 interaction unknown at this stage
    • In vivo phenotype of CHIP loss not yet characterized
    • Ubiquitin chain-type specificity not resolved
  3. 2004 High

    Translation of CHIP's quality-control function to neurodegeneration was achieved by showing CHIP ubiquitinates tau in an Hsp70/Hsp90-dependent manner and is found at tau lesions in human tauopathy brain, directly linking chaperone-dependent ubiquitination to a disease-relevant substrate.

    Evidence In vivo ubiquitination, geldanamycin/heat-shock Hsp70 induction, tau aggregation assay, immunohistochemistry on human postmortem brain, transgenic mice

    PMID:14962978

    Open questions at the time
    • Which tau phospho-species are preferentially targeted was unclear
    • Whether CHIP is sufficient or necessary in vivo for tau clearance not proven
    • Mechanism of CHIP at tau aggregates versus soluble tau not distinguished
  4. 2007 High

    A key refinement was that the HSP90-CHIP axis selectively recognizes phosphorylated tau (p-tau) for ubiquitination and degradation, with Hsp90 inhibitors reducing p-tau in a tauopathy mouse model in a CHIP-dependent manner, establishing p-tau as the preferred physiological substrate of the CHIP-chaperone axis.

    Evidence In vitro ubiquitination, Hsp90 inhibitor treatment, CHIP knockdown, tauopathy mouse model

    PMID:17304350

    Open questions at the time
    • Precise phospho-degron on tau not yet mapped
    • Relative contributions of Hsp70 vs Hsp90 in delivering p-tau to CHIP not resolved
    • Therapeutic window of Hsp90 inhibitors for p-tau clearance in humans unknown
  5. 2008 High

    The discovery that Akt is itself a CHIP substrate competing with tau for Hsp90/CHIP-mediated ubiquitination revealed a feedback loop in which cellular kinase signaling tunes CHIP's substrate selectivity, adding a layer of regulation to chaperone-assisted quality control.

    Evidence Co-IP, ubiquitination assay, Akt1 knockout mice, kinase activity assay

    PMID:18292230

    Open questions at the time
    • Whether other kinase clients similarly compete for CHIP access not tested
    • Stoichiometric basis of Akt-tau competition at Hsp90 not quantified
  6. 2013 Medium

    CHIP's role expanded beyond proteostasis when it was shown to ubiquitinate NF-κB p65 for degradation (dampening pro-tumorigenic signaling) and to catalyze non-degradative K27-linked ubiquitination of CARMA1 to activate NF-κB in T cells, demonstrating that CHIP can both suppress and activate the same pathway depending on context and ubiquitin-chain topology.

    Evidence Co-IP, ubiquitination assays with chain-type specificity, NF-κB reporters, xenograft tumor model, T-cell IL-2 production

    PMID:23322406 PMID:24302614

    Open questions at the time
    • How CHIP selects between K27 and K48 linkages mechanistically is unknown
    • Whether CARMA1 K27-ubiquitination by CHIP occurs in vivo in animal models not shown
    • Opposing NF-κB effects not integrated into a unified model
  7. 2014 High

    CHIP was placed at the center of cytokine receptor turnover and immune homeostasis: it ubiquitinates IL-4Rα for proteasomal degradation, and STUB1-knockout mice develop spontaneous airway inflammation and elevated IgE, demonstrating an in vivo requirement for CHIP in restraining type-2 immune responses.

    Evidence Co-IP, flow cytometry, STUB1 knockout mice with lung inflammation phenotyping

    PMID:24251647

    Open questions at the time
    • Whether CHIP similarly regulates other cytokine receptor family members in vivo not tested
    • Cell-type-specific contributions of CHIP in immune regulation not dissected
  8. 2017 High

    A paradoxical finding resolved how CHIP loss impairs autophagy: CHIP preferentially ubiquitinates inactive (mTOR-phosphorylated) TFEB for proteasomal degradation; in STUB1-KO mice, phosphorylated TFEB accumulates and overall TFEB transcriptional activity decreases, reducing autophagy and mitochondrial biogenesis—revealing CHIP as a gatekeeper that removes the inactive pool to promote active TFEB signaling.

    Evidence STUB1-KO cells and mice, TFEB phosphorylation analysis, ubiquitination assay, autophagy flux and mitochondrial biogenesis measurements

    PMID:28754656

    Open questions at the time
    • Whether CHIP-mediated TFEB regulation is tissue-specific not explored
    • Structural basis for selective recognition of phospho-TFEB not determined
  9. 2020 High

    CHIP was established as the E3 ligase for proteaphagy: it attaches K63-linked ubiquitin chains to inhibited 26S proteasomes, which are then transported via HDAC6/dynein to aggresomes and cleared by macroautophagy, providing the first mechanistic link between a specific E3 ligase and mammalian proteasome disposal.

    Evidence In vitro ubiquitylation of purified human 26S proteasomes, K63-linkage determination, STUB1-KO and chemical inhibition, HDAC6/dynein perturbation, LC3/SQSTM1 colocalization

    PMID:32723828

    Open questions at the time
    • Receptor/adaptor linking K63-ubiquitinated proteasomes to autophagy machinery not fully identified
    • Whether proteaphagy via CHIP is relevant in neurons and to SCAR16 pathology not tested
  10. 2021 High

    A genome-wide CRISPR screen identified STUB1 as a negative regulator of IFNγ signaling by ubiquitinating IFNγ-R1 (K285) and JAK1 (K249) for proteasomal degradation; STUB1 loss amplified IFNγ responsiveness and sensitized tumors to cytotoxic T-cell killing, positioning CHIP as a target in cancer immunotherapy.

    Evidence CRISPR/Cas9 screen, site-specific mutagenesis, ubiquitination assay, cytotoxic T-cell killing assay

    PMID:35395848

    Open questions at the time
    • Whether STUB1 inhibition improves checkpoint immunotherapy in vivo not demonstrated
    • Chaperone-dependence of IFNγ-R1/JAK1 ubiquitination by CHIP not tested
  11. 2023 High

    Biophysical and cellular dissection of the CHIP–tau interaction showed that CHIP's TPR domain binds phosphorylated tau ~10-fold more tightly than unmodified tau via a partially distinct binding mode, identifying a phosphorylation-dependent degron and confirming that sub-stoichiometric CHIP potently suppresses p-tau aggregation and seeding.

    Evidence In vitro binding panel (TPR-domain chaperones), aggregation and seeding assays with purified proteins, cellular seeding assay

    PMID:37330289

    Open questions at the time
    • Structural details of the phospho-degron recognition interface not resolved at atomic resolution
    • In vivo validation in tauopathy models not included
  12. 2023 Medium

    CHIP's substrate repertoire expanded to include key RNA/epitranscriptomic regulators (AGO2, Dicer, METTL14, YTHDF2) and the ferroptosis regulator GPX4, with site-specific ubiquitination mapped for each, connecting CHIP to antiviral RNAi, m6A RNA modification homeostasis, and ferroptotic cell death.

    Evidence Co-IP, K48-linkage ubiquitination assays, site-specific mutagenesis, STUB1-KO mouse antiviral model, m6A MeRIP-seq, ferroptosis lipid ROS and iron measurements

    PMID:35533808 PMID:36597993 PMID:37515378 PMID:38110356

    Open questions at the time
    • Chaperone-dependence of each new substrate ubiquitination not always demonstrated
    • Relative physiological importance of these substrates versus classical chaperone clients unknown
    • Each substrate reported by a single lab
  13. 2024 Medium

    Post-translational regulation of CHIP itself was dissected: BCKDK phosphorylates CHIP at S19 to disrupt BCAT1 interaction, and KAT5-mediated histone acetylation drives STUB1 transcription, demonstrating that both transcriptional and post-translational inputs modulate CHIP activity toward specific substrates in disease contexts (GBM, myocardial ischemia).

    Evidence Site-specific phospho-mutagenesis, KAT5 overexpression, Co-IP, ubiquitination assay, in vivo GBM and MIRI models

    PMID:38561411 PMID:38621458

    Open questions at the time
    • Comprehensive map of CHIP's own PTMs and their functional consequences lacking
    • Whether S19 phosphorylation globally affects CHIP activity or is BCAT1-specific unknown
    • Both studies from single labs

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include the atomic-resolution structural basis for CHIP's selective recognition of phosphorylated substrates, the mechanisms determining ubiquitin chain-type selection (K48 vs K63 vs K27), the tissue-specific in vivo contributions of CHIP to immune regulation and neurodegeneration (particularly the mechanistic basis of SCAR16/SCA48 cerebellar pathology), and whether CHIP inhibition can be therapeutically exploited to enhance anti-tumor immunity.
  • No high-resolution structure of CHIP bound to a phosphorylated substrate
  • Chain-type selectivity determinants not mechanistically elucidated
  • SCAR16/SCA48 disease mechanism at the cellular level incompletely understood

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 17 GO:0016874 ligase activity 4 GO:0044183 protein folding chaperone 3 GO:0098772 molecular function regulator activity 3
Localization
GO:0005829 cytosol 3 GO:0005634 nucleus 2
Pathway
R-HSA-392499 Metabolism of proteins 12 R-HSA-8953897 Cellular responses to stimuli 6 R-HSA-162582 Signal Transduction 5 R-HSA-168256 Immune System 5 R-HSA-1643685 Disease 4 R-HSA-9612973 Autophagy 3 R-HSA-5357801 Programmed Cell Death 2 R-HSA-9909396 Circadian clock 1
Partners
HSP90AA1HSPA1AHSPA8IFNGR1JAK1MAPTTFEBUBE2D1

Evidence

Reading pass · 37 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1999 CHIP (STUB1) was identified as a novel 35-kDa cytoplasmic protein that directly interacts with Hsc70 and Hsp70 via its N-terminal tetratricopeptide repeat (TPR) domain; it inhibits Hsp40-stimulated ATPase activity of Hsc70/Hsp70 and reduces chaperone efficiency for substrate refolding, establishing it as a negative regulator of the Hsc70/Hsp70 chaperone cycle. Yeast two-hybrid screen, in vitro GST pulldown, co-immunoprecipitation from human skeletal muscle cells, ATPase activity assay, luciferase refolding assay Molecular and cellular biology High 10330192
2001 CHIP acts as a U-box-dependent E3 ubiquitin ligase that works with the E2 UbcH5 family; it ubiquitylates its co-chaperone substrate Hsc70 (with short non-canonical chains) and promotes ubiquitin-dependent degradation of chaperone substrates, establishing the U-box as the catalytic domain for E3 activity. In vitro ubiquitylation assay with recombinant proteins, U-box deletion mutagenesis, co-immunoprecipitation The Journal of biological chemistry High 11557750
2001 CHIP is a chaperone-dependent E3 ligase that selectively ubiquitylates unfolded (thermally denatured) proteins captured by Hsp90 or Hsc70/Hsp40, but not folded proteins, using Ubc4/UbcH5c as E2; CHIP lacking its U-box shows no activity, demonstrating U-box requirement for ubiquitylation of misfolded substrates. In vitro ubiquitylation assay with denatured luciferase as substrate, U-box deletion mutant EMBO reports High 11743028
2001 CHIP interacts with Hsp90 via its TPR domain, incorporates into Hsp90 heterocomplexes, elicits release of the regulatory cofactor p23, abolishes glucocorticoid receptor steroid-binding activity and transactivation, and induces glucocorticoid receptor ubiquitylation and proteasomal degradation, remodeling Hsp90 complexes toward substrate degradation rather than folding. Co-immunoprecipitation, in vivo ubiquitylation assay, glucocorticoid receptor transactivation assay, proteasome inhibitor rescue Nature cell biology High 11146632
2001 CHIP functions with Hsc70 to sense the folded state of CFTR and targets aberrant (misfolded) CFTR for proteasomal degradation by promoting its ubiquitination; overexpression of U-box-deleted CHIP inhibited endogenous CHIP and blocked CFTR ubiquitination, demonstrating that CHIP converts Hsc70 into a degradation factor for ER quality control. Co-immunoprecipitation, ubiquitination assay, dominant-negative U-box deletion mutant overexpression, proteasome inhibitor rescue Nature cell biology High 11146634
2004 CHIP directly ubiquitinates the microtubule-associated protein tau in a manner dependent on its interaction with Hsp70/90; induction of Hsp70 (via geldanamycin or heat shock) decreases tau steady-state levels and selectively reduces detergent-insoluble tau, while CHIP also promotes tau aggregation. Diverse tau lesions in human postmortem tissue are immunopositive for CHIP. In vivo ubiquitination assay, Hsp70 induction (geldanamycin/heat shock), tau aggregation assay, immunohistochemistry on human brain tissue, transgenic mouse overexpression Human molecular genetics High 14962978
2007 The high-affinity HSP90-CHIP complex selectively recognizes and degrades phosphorylated tau (p-tau); Hsp90 inhibition reduces p-tau levels in a CHIP-dependent manner independent of HSF1 activation, and cochaperones of the mature Hsp90 refolding complex antagonize this effect. Peripheral administration of an Hsp90 inhibitor selectively reduced p-tau species in a mouse tauopathy model. In vitro ubiquitination, HSP90 inhibitor treatment (geldanamycin derivatives), CHIP knockdown, tauopathy mouse model, western blotting The Journal of clinical investigation High 17304350
2008 CHIP and Akt co-regulate tau degradation: Akt is ubiquitinated and degraded by CHIP in an Hsp90-dependent manner; Akt prevents CHIP-induced tau ubiquitination by competing as a client protein or by directly regulating the Hsp90/CHIP complex; Akt levels tightly regulate CHIP levels via a stress-response feedback; Akt enhances PAR1/MARK2 kinase activity to promote tau hyperphosphorylation at S262/S356, a species not recognized by CHIP/Hsp90. Co-immunoprecipitation, ubiquitination assay, Akt1 knockout mice, kinase activity assay, western blotting Proceedings of the National Academy of Sciences of the United States of America High 18292230
2010 CHIP/STUB1 ubiquitinates and promotes degradation of mutant keratins (K14-p.Arg125Cys) via its TPR-domain-dependent interaction with Hsc70 and Hsp70; deletion of the TPR domain (DeltaTPR-CHIP) blocked mutant keratin degradation, and CHIP overexpression strongly reduced keratin aggregates. CHIP overexpression/dominant-negative TPR deletion mutant, immunofluorescence, western blotting in EBS cell models and K5-/- neonatal mice Human mutation Medium 20151404
2011 STUB1/CHIP regulates NQO1 protein levels by interacting with NQO1 via its TPR domain and ubiquitinating it for proteasomal degradation; the NQO1 polymorphic variant P187S (C609T) is a stronger STUB1 interactor with increased susceptibility to ubiquitination. Age-dependent decrease of STUB1 correlates with increased NQO1 accumulation in brain. Co-immunoprecipitation, in vivo ubiquitination assay, western blotting in CHIP-knockout cells and aged mouse brain, human Alzheimer's disease hippocampal tissue analysis The Journal of biological chemistry Medium 21220432
2012 miR-764-5p promotes osteoblast differentiation by suppressing CHIP/STUB1 translation via targeting its 3'-UTR, leading to decreased CHIP protein levels; CHIP negatively regulates osteoblast differentiation by promoting Runx2 protein degradation, and forced miR-764-5p expression is reversed by CHIP overexpression. miRNA overexpression/inhibition, 3'-UTR reporter assay, CHIP overexpression/knockdown, osteoblast differentiation assay Journal of bone and mineral research Medium 22407479
2013 CHIP/STUB1 negatively regulates NF-κB signaling in colorectal cancer cells by promoting ubiquitination and proteasomal degradation of p65 (RelA), a subunit of the NF-κB complex, leading to decreased expression of NF-κB targets (Cyclin D1, c-Myc, MMP-2, VEGF, IL-8) and impaired tumor growth and invasion. CHIP overexpression/knockdown, ubiquitination assay, co-immunoprecipitation, NF-κB reporter assay, xenograft tumor model Carcinogenesis Medium 24302614
2013 STUB1 is essential for T-cell activation: it constitutively interacts with CARMA1 (an adaptor protein linking antigen receptors to NF-κB), an interaction intensified by TCR stimulation; STUB1 catalyzes Lys-27-linked ubiquitination of CARMA1, which is required for CARMA1-mediated NF-κB activation and IL-2 production. Co-immunoprecipitation, RNAi knockdown, NF-κB reporter assay, ubiquitin linkage-specific analysis, IL-2 ELISA European journal of immunology Medium 23322406
2014 STUB1 interacts with and targets IL-4Rα for ubiquitination-mediated proteasomal degradation, terminating IL-4/IL-13 signaling; STUB1 knockout cells show increased IL-4Rα levels and sustained STAT6 activation; STUB1-deficient mice exhibit spontaneous airway inflammation, alternative M2 macrophage activation, and increased serum IgE. Co-immunoprecipitation, flow cytometry, immunoblot, STUB1 knockout mice, lung inflammation phenotyping American journal of respiratory and critical care medicine High 24251647
2014 Hsp70 and Hsp90 oppositely regulate TGF-β signaling through CHIP/STUB1: Hsp70 overexpression or Hsp90 inhibition (geldanamycin) facilitates CHIP-induced ubiquitination and degradation of Smad3, enhancing TGF-β signaling; Hsp90 overexpression antagonizes CHIP-mediated Smad3 ubiquitination, desensitizing cells to TGF-β. Co-immunoprecipitation, ubiquitination assay, Hsp90 inhibitor treatment, Smad3 overexpression/knockdown, TGF-β signaling reporter Biochemical and biophysical research communications Medium 24613385
2014 CHIP/STUB1 directly interacts with eIF5A preferentially via its U-box domain, mediates eIF5A ubiquitination and proteasomal degradation; CHIP expression inversely correlates with eIF5A levels in colorectal cancers and in CHIP-knockout MEF cells. Proteomics/co-IP identification, direct interaction assay, ubiquitination assay, CHIP-KO MEF cells, western blotting of colorectal cancer specimens Cellular signalling Medium 24509416
2015 CHIP/STUB1 regulates autophagic flux: CHIP knockdown increases autophagosome formation by elevating PTEN levels and decreasing AKT/mTOR activity (reducing ULK1 Ser757 phosphorylation), but also impairs autophagic substrate (p62) degradation and increases susceptibility to autophagic cell death induced by bafilomycin A1. CHIP knockdown (RNAi), LC3 and p62 western blotting, AKT/mTOR/ULK1 phosphorylation analysis, bafilomycin A1 treatment Neuroscience bulletin Medium 26219223
2017 STUB1 modulates TFEB activity by preferentially ubiquitinating inactive, phosphorylated TFEB (phosphorylated by mTOR) for proteasomal degradation; STUB1-deficient cells and STUB1-KO mouse tissues accumulate phosphorylated TFEB, resulting in reduced TFEB transcriptional activity, reduced autophagy, and reduced mitochondrial biogenesis; STUB1 overexpression reduces phosphorylated TFEB and increases TFEB activity. STUB1 knockout cells and mice, TFEB phosphorylation analysis, co-immunoprecipitation, ubiquitination assay, autophagy flux assay, mitochondrial biogenesis measurement The EMBO journal High 28754656
2017 STUB1 binds to RUNX1 and induces its ubiquitination and degradation mainly in the nucleus; STUB1-induced ubiquitination also promotes nuclear export of RUNX1, reducing its transcriptional activity; STUB1 also ubiquitinates the leukemic fusion protein RUNX1-RUNX1T1 and inhibits its expression, with STUB1 overexpression showing growth-inhibitory effects selectively in RUNX1-RUNX1T1 leukemia cells. High-throughput E3 ligase binding assay, co-immunoprecipitation, ubiquitination assay, immunofluorescence for nuclear export, cell growth assay in leukemia lines The Journal of biological chemistry Medium 28536267
2018 In advanced prostate cancer, STUB1 interacts with the HSP70 complex to mediate AR and AR-V7 ubiquitination and degradation; STUB1 disassociates AR/AR-V7 from HSP70 to facilitate their proteasomal degradation; HSP70 inhibition restores STUB1-mediated AR/AR-V7 suppression and re-sensitizes resistant tumors to enzalutamide/abiraterone. Co-immunoprecipitation, ubiquitination assay, HSP70 inhibitor treatment, xenograft tumor model, western blotting in enzalutamide/abiraterone-resistant cell lines Nature communications High 30446660
2019 STUB1 suppresses YAP1 signaling in cancer: STUB1 directly ubiquitinates YAP1 at K280 via K48-linked polyubiquitination, promoting YAP1 proteasomal degradation; low STUB1 expression correlates with increased YAP1 protein in gastric cancer; STUB1-mediated YAP1 degradation increases cellular chemosensitivity. Co-immunoprecipitation, ubiquitination assay with site-specific K280 mutation, western blotting, chemosensitivity assay, gastric cancer patient sample analysis Cancer science Medium 31393050
2019 STUB1 deficiency leads to intracellular accumulation of protein aggregates and increased secretion of small extracellular vesicles (exosomes) enriched in ubiquitinated and/or undegraded proteins; oxidative stress further increases exosome release in STUB1-depleted cells, revealing a cooperative mechanism between STUB1-mediated proteostasis and exosome-based disposal of proteotoxic material. STUB1 knockdown, nanoparticle tracking analysis of exosomes, western blotting for ubiquitinated cargo, oxidative stress assay PloS one Medium 31613922
2020 STUB1 specifically ubiquitylates purified human 26S proteasomes in vitro via Lys63-linked chains; inhibited proteasomes are sequestered into aggresomes via HDAC6- and dynein-mediated transport and cleared through selective macroautophagy (proteaphagy); genetic and chemical inhibition of STUB1 significantly impaired proteasome processing and reduced resistance to proteasomal stress. In vitro ubiquitylation of purified human proteasomes, genetic STUB1 KO and chemical inhibition, HDAC6/dynein inhibition, SQSTM1/LC3 colocalization, proteasome activity assay Proceedings of the National Academy of Sciences of the United States of America High 32723828
2020 STUB1 ubiquitinates and degrades BMAL1 (core circadian clock protein) via K48-linked polyubiquitin chains promoting proteasomal degradation; STUB1 and BMAL1 interaction domains were identified; oxidative stress promotes STUB1 nuclear translocation and enhanced co-localization with BMAL1; STUB1 expression attenuates hydrogen peroxide-induced cell senescence in a BMAL1-dependent manner. Affinity purification and MS, co-immunoprecipitation, ubiquitination assay (K48-linkage), STUB1 nuclear translocation imaging, senescence-associated β-gal staining, BMAL1 knockdown/overexpression rescue The Journal of biological chemistry Medium 32041778
2020 PDLIM5 protects SMAD3 from STUB1-mediated proteasomal degradation: PDLIM5 interacts with SMAD3 (but not SMAD2) and competitively suppresses the interaction between SMAD3 and STUB1; PDLIM5 knockdown reduces SMAD3 levels, which is rescued by STUB1 knockdown, establishing STUB1 as the E3 ligase for basal SMAD3 stability in NSCLC. Co-immunoprecipitation, competitive binding assay, STUB1 knockdown rescue, ubiquitination assay, migration/invasion assay The Journal of biological chemistry Medium 32737199
2021 STUB1 mediates ubiquitination-dependent proteasomal degradation of IFNγ-R1 in complex with its signal-relaying kinase JAK1; ubiquitination occurs at IFNγ-R1 K285 and JAK1 K249; STUB1 inactivation amplifies IFNγ signaling and sensitizes tumor cells to cytotoxic T cells in vitro; identified via genome-wide CRISPR/Cas9 screen. Genome-wide CRISPR/Cas9 screen, co-immunoprecipitation, site-specific mutagenesis (K285R, K249R), ubiquitination assay, cytotoxic T cell killing assay, IFNγ signaling (STAT1) measurement Nature communications High 35395848
2021 TRIM6 promotes breast cancer progression by interacting with STUB1 and promoting ubiquitination-mediated degradation of STUB1, which in turn increases YAP1 protein levels; STUB1 overexpression attenuates TRIM6-induced breast cancer growth, placing STUB1 as a substrate of TRIM6 and an upstream suppressor of YAP1. Co-immunoprecipitation, ubiquitination assay, TRIM6/STUB1 overexpression/knockdown, in vitro and in vivo tumor growth assays European journal of histochemistry Medium 33728863
2022 STUB1 ubiquitinates the transcription factor RFX1 via polyubiquitination for proteasomal degradation in SLE T cells; STUB1 is upregulated in CD4+ T cells from SLE patients; STUB1 overexpression in CD4+ T cells leads to upregulation of CD70 and CD11a (RFX1 target genes implicated in SLE pathogenesis). Ubiquitination assay, western blotting, STUB1 overexpression in CD4+ T cells, CD70/CD11a flow cytometry, SLE patient samples Clinical immunology Medium 27283392
2022 STUB1 promotes non-degradative K63-linked ubiquitination of the aryl hydrocarbon receptor (AHR) in T cells, facilitating Th17/Treg imbalance in rheumatoid arthritis; STUB1 overexpression upregulates Th17 markers and downregulates Treg markers; ubiquitination sites on AHR responsible for STUB1-mediated K63 chain modification were identified. Western blot, flow cytometry, siRNA knockdown/overexpression, EROD enzymatic activity assay for AHR function, ubiquitin linkage-specific analysis, RA patient samples Clinical and experimental immunology Medium 35943876
2022 STUB1 regulates the RNAi machinery by directly interacting with and ubiquitinating AGO2 (and AGO1, AGO3, AGO4) via K48-linked polyubiquitin chains for proteasomal degradation in a chaperone-dependent manner; STUB1 also induces K48-linked ubiquitination and degradation of Dicer and antiviral Dicer (aviDicer); STUB1 deficiency upregulates Dicer and AGO2, enhancing antiviral RNAi and inhibiting Enterovirus A71 replication in newborn mice. Co-immunoprecipitation, K48-linkage ubiquitination assay, STUB1 KO cells and newborn mouse model of EV-A71 infection, virus-derived siRNA quantification Virologica Sinica Medium 35533808
2023 STUB1/CHIP binds 10-fold more strongly to phosphorylated tau than unmodified tau via its TPR domain (in a partially distinct binding mode); sub-stoichiometric concentrations of CHIP strongly suppress aggregation and seeding of phosphorylated tau; CHIP promotes rapid ubiquitination of phosphorylated tau but not unmodified tau in vitro; in cells, CHIP restricts seeding by phosphorylated tau, identifying a phosphorylation-dependent degron on tau. In vitro binding assay (panel of TPR-domain chaperones), aggregation assay, seeding assay, in vitro ubiquitination, cellular seeding assay Journal of molecular biology High 37330289
2023 METTL3 protects METTL14 from STUB1-mediated proteasomal degradation: STUB1 directly interacts with METTL14 and ubiquitinates it at K148, K156, and K162; METTL3 regions 450–454 and 464–480 are essential for competing with STUB1 to stabilize METTL14, thereby maintaining m6A homeostasis; changes in STUB1 expression affect m6A levels and tumorigenesis. Co-immunoprecipitation, ubiquitination assay with site-specific mutagenesis (K148/156/162R), METTL3 domain deletion mapping, m6A dot blot and MeRIP-seq, tumorigenesis assay EMBO reports Medium 36597993
2023 HSP90β impedes STUB1-induced ubiquitination and degradation of YTHDF2 in hepatocellular carcinoma: HSP90β physically interacts with both STUB1 and YTHDF2 via its middle domain; HSP90β inhibits STUB1-mediated YTHDF2 degradation, thereby boosting HCC proliferation and sorafenib resistance. Co-immunoprecipitation, domain-mapping (HSP90β large and small middle domain), ubiquitination assay, HSP90β knockdown/overexpression, YTHDF2 protein stability assay, sorafenib resistance assay Advanced science Medium 37515378
2023 STUB1 promotes ferroptosis in gastrointestinal stromal tumors by ubiquitinating GPX4 at K191, leading to its degradation; imatinib treatment increases STUB1-mediated GPX4 ubiquitination; GPX4 overexpression or STUB1 knockdown reverses imatinib-induced ferroptosis. STUB1 knockdown/GPX4 overexpression, site-specific K191 ubiquitination mutagenesis, lipid ROS and Fe2+ measurement, RSL3 combination treatment in vivo and in vitro Cell death & disease Medium 38110356
2024 STUB1 is the E3 ubiquitin ligase for BCAT1, mediating its ubiquitination for proteasomal degradation; BCKDK phosphorylates BCAT1 at S5, S9, and T312 to stabilize it, and also phosphorylates STUB1 at S19 to disrupt its interaction with BCAT1, thereby inhibiting BCAT1 degradation; this BCKDK-STUB1-BCAT1 axis promotes GBM progression. Co-immunoprecipitation, ubiquitination assay, site-specific phospho- and ubiquitin-mutagenesis, in vivo and in vitro GBM models, temozolomide sensitivity assay Cancer letters Medium 38621458
2024 KAT5 acetyltransferase promotes STUB1 transcription via histone acetylation; STUB1 then ubiquitinates LATS2 for proteasomal degradation, activating the YAP/β-catenin pathway; in myocardial ischemia-reperfusion injury, the KAT5/STUB1/LATS2/YAP/β-catenin axis suppresses NLRP3-mediated cardiomyocyte pyroptosis. KAT5/STUB1 overexpression, LATS2 knockdown/overexpression, co-immunoprecipitation, ubiquitination assay, YAP/β-catenin signaling assay, MIRI oxygen-glucose deprivation model and in vivo LAD ligation Communications biology Medium 38561411
2024 STUB1 ubiquitinates the RNA methyltransferase NSUN2 at K457 and K654, promoting its proteasomal degradation during ferroptosis; loss of NSUN2 reduces m5C methylation of GPX4 mRNA 3'UTR, abrogating SBP2 interaction with the SECIS element and inhibiting GPX4 protein expression, thereby promoting hepatocyte ferroptosis. Co-immunoprecipitation, site-specific ubiquitination mutagenesis (K457R/K654R), m5C MeRIP, SBP2-SECIS interaction assay, GPX4 western blotting, ferroptosis assays in vivo and in vitro Cell reports Medium 39453812

Source papers

Stage 0 corpus · 130 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2006 Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 2861 17081983
2012 Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 1718 22658674
2005 A human protein-protein interaction network: a resource for annotating the proteome. Cell 1704 16169070
2002 Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America 1479 12477932
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