Affinage

TAB3

TGF-beta-activated kinase 1 and MAP3K7-binding protein 3 · UniProt Q8N5C8

Length
712 aa
Mass
78.7 kDa
Annotated
2026-06-10
48 papers in source corpus 21 papers cited in narrative 21 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

TAB3 is an ubiquitin-binding adaptor that couples innate immune and inflammatory receptors to the kinase TAK1, driving activation of NF-κB and MAPK pathways (PMID:14633987, PMID:14670075). It associates constitutively with TAK1 (in complex with TAB1) and, upon stimulation, bridges receptor-proximal ubiquitin signals to the kinase: endogenous TAB3 interacts with TRAF6 in an IL-1-dependent manner and with TRAF2 in a TNF-dependent manner and is itself ubiquitinated by TRAF6 (PMID:14633987), while two parallel TAK1-TAB1-TAB2 and TAK1-TAB1-TAB3 complexes are engaged by TNFα, IL-1, and LPS (PMID:14670075). The defining biochemical activity is preferential recognition of Lys63-linked polyubiquitin chains through its NZF/zinc-finger domain, which engages distal and proximal ubiquitins via a conserved Thr-Phe dipeptide and the Ile44 hydrophobic patch respectively; this binding is essential for TAK1 and IKK activation (PMID:15327770, PMID:19927120), and is specifically required for sustained TAK1 signaling and downstream JNK and p38 activation (PMID:28507161). TAB3 binds TAK1 through a non-contiguous C-terminal region (residues 479–553), and competition with this region blocks TAK1 phosphorylation and downstream IKK/MAPK activation, RANKL-induced osteoclast differentiation, and related outputs (PMID:17158449). TAB3 function extends across TLR, CD40, and B-cell receptor signaling—where it links TAK1 to CARMA1 to drive IKK activation (PMID:27497262) and, redundantly with TAB2, supports B-cell development and macrophage pro-inflammatory cytokine production via IκBζ (PMID:23509369, PMID:38567483)—and in some contexts drives MAPK activation independently of TAK1 (PMID:23509369, PMID:30760523). TAB3 is heavily regulated: p38α phosphorylates it at Ser60, Thr404, and Ser506 in a TAB1-dependent manner (PMID:14670075, PMID:18021073); its protein and mRNA stability are controlled by TRIM30α-mediated degradation (PMID:18345001), USP15-dependent protection from NBR1 autophagic degradation (PMID:31903660), and METTL3/IGF2BP2 m6A modification of its transcript (PMID:35417191); and Smad7 antagonizes its assembly into TAK1 complexes (PMID:17384642). Beyond its kinase-scaffolding role, TAB3 constitutively inhibits autophagy by sequestering Beclin 1 through coiled-coil-domain interactions, releasing it upon autophagy induction to instead engage TAK1 (PMID:22081109).

Mechanistic history

Synthesis pass · year-by-year structured walk · 16 steps
  1. 2003 High

    Established TAB3 as a TAK1-binding adaptor that links inflammatory receptors to NF-κB, answering whether a TAB2-like protein bridges IL-1/TNF signals to the kinase.

    Evidence Co-IP, siRNA double-knockdown, and NF-κB reporter assays in mammalian cells

    PMID:14633987

    Open questions at the time
    • Did not define the ubiquitin-binding basis of recruitment
    • Redundancy with TAB2 left individual contributions unresolved
  2. 2004 High

    Identified Lys63-polyubiquitin binding by the zinc-finger domain as the essential molecular activity for signaling, explaining how TAB3 senses receptor-proximal ubiquitination.

    Evidence In vitro binding, ZnF mutagenesis, and heterologous ubiquitin-binding-domain swap rescue with IKK activation readouts

    PMID:15327770

    Open questions at the time
    • Structural basis of chain-linkage selectivity not yet resolved
    • Did not address chain-length requirements in cells
  3. 2004 High

    Resolved that TAB3 forms a distinct TAK1-TAB1-TAB3 complex parallel to the TAB2 complex and is phosphorylated via p38α upon stimulation, framing TAB3 as both effector and substrate.

    Evidence Co-IP, phosphatase treatment, SB203580 inhibition, and p38α-knockout MEFs

    PMID:14670075

    Open questions at the time
    • Functional consequence of phosphorylation undefined at this stage
    • Specific phosphosites not mapped
  4. 2006 High

    Mapped the TAB3-binding interface on TAK1 to a non-contiguous C-terminal region, providing a dominant-negative tool that confirmed TAB3-TAK1 binding is required for receptor-driven IKK/MAPK output and osteoclast differentiation.

    Evidence Deletion mapping, dominant-negative competition, kinase assays, osteoclast differentiation assays

    PMID:17158449

    Open questions at the time
    • Did not establish stoichiometry or whether binding is direct in vitro
  5. 2007 High

    Revealed Smad7 as a TGF-β-induced antagonist that blocks TAB3 incorporation into TRAF2-TAK1 complexes, connecting TAB3 to crosstalk between TGF-β and NF-κB signaling.

    Evidence Co-IP and Smad7-transgenic mouse skin with NF-κB translocation assays

    PMID:17384642

    Open questions at the time
    • Binding interface on TAB3 for Smad7 not mapped
  6. 2008 High

    Defined TRIM30α as a TLR-induced negative-feedback regulator that degrades TAB3, and mapped p38α/MAPKAP-K2 phosphosites (Ser60, Thr404, Ser506), establishing layered post-translational control of TAB3.

    Evidence Co-IP, siRNA, transgenic/endotoxic-shock mice (TRIM30α); MS phosphosite mapping and TAB1-knockout MEFs (phosphorylation)

    PMID:18021073 PMID:18345001

    Open questions at the time
    • Functional output of each phosphosite on TAK1 activity not fully dissected
    • Whether TRIM30α ubiquitinates TAB3 directly unresolved
  7. 2009 High

    Provided atomic-resolution structures of the TAB3 NZF domain bound to Lys63-diubiquitin, defining the distal Thr-Phe and proximal Ile44 contacts that confer chain-linkage specificity.

    Evidence X-ray crystallography at 1.4 Å with site-directed mutagenesis and ubiquitin-binding assays

    PMID:19927120

    Open questions at the time
    • Structure of the full TAB3-TAK1 assembly on polyubiquitin not determined
  8. 2011 High

    Uncovered a TAK1-independent moonlighting function: TAB3 constitutively sequesters Beclin 1 to suppress autophagy, dissociating upon induction, linking inflammatory signaling components to autophagy control.

    Evidence Co-IP, coiled-coil-domain mapping, overexpression/siRNA with EM and GFP-LC3 autophagy readouts

    PMID:22081109

    Open questions at the time
    • Signal triggering TAB3-Beclin 1 dissociation not identified
    • Physiological relevance in vivo not established here
  9. 2013 High

    Showed TAB3 (with TAB2) drives B-cell MAPK activation and B-1/marginal-zone development through a surprising TAK1-independent route, distinguishing its MAPK and NF-κB functions.

    Evidence Conditional double-knockout mice, B-cell stimulation, MAPK/NF-κB activation assays

    PMID:23509369

    Open questions at the time
    • Identity of the TAK1-independent effector kinase unknown
    • Individual TAB3 vs TAB2 contributions not separated
  10. 2014 High

    Demonstrated that enterovirus 71 3C protease cleaves TAB3 at defined sites to dismantle the TAK1 complex and suppress NF-κB, identifying TAB3 as a viral immune-evasion target.

    Evidence Protease assays, active-site mutagenesis, cleavage-site mapping, Co-IP, NF-κB reporters

    PMID:24942571

    Open questions at the time
    • Contribution of TAB3 cleavage relative to other complex members not quantified
  11. 2017 High

    Genetically separated two modes of TAK1 activation, establishing that TAB3-mediated K63-ubiquitin binding is specifically required for sustained TAK1 signaling and JNK/p38γ activation.

    Evidence TAB2/3 double-KO and TAB1/2/3 triple-KO cells with ubiquitin-binding-defective rescue and kinase assays

    PMID:28507161

    Open questions at the time
    • Mechanism of the transient TAB-independent TAK1 activation mode unresolved
  12. 2016 Medium

    Extended TAB3 function to antigen-receptor signaling, showing it links TAK1 to CARMA1 for BCR-induced IKK activation, and identified O-GlcNAcylation at Ser408 as a PTM gating Thr404 phosphorylation and TAK1 activation in cancer cells.

    Evidence TAB2/3-deficient DT40 cells with domain-deletion mutants (BCR/CARMA1); O-GlcNAc site mapping with OGT co-expression and kinase assays (Ser408)

    PMID:27009840 PMID:27497262

    Open questions at the time
    • Each from single labs without independent replication
    • Direct CARMA1-TAB3 contact vs bridging not distinguished
  13. 2019 Medium

    Described a non-canonical TAB1-TAB3-dependent p38 activation pathway downstream of GPCR agonists in endothelial cells, bypassing MKK3/MKK6.

    Evidence siRNA knockdown with p38/MKK phosphorylation and IL-6 readouts across endothelial cell types

    PMID:30760523

    Open questions at the time
    • Single lab
    • Direct biochemical mechanism of MKK bypass not shown
  14. 2020 Medium

    Defined two post-transcriptional/post-translational stability controls and oncogenic signaling roles: USP15 protects TAB3 from NBR1 autophagic degradation (deubiquitinase-independent), and TAB3 drives STAT3/PIM1 signaling in colorectal cancer.

    Evidence Co-IP, autophagy-degradation assays, deubiquitinase-dead mutant (USP15); Co-IP, siRNA rescue, xenograft (STAT3/PIM1)

    PMID:31903660 PMID:32229191

    Open questions at the time
    • Single labs
    • Direct vs indirect TAB3-STAT3 association not fully resolved
  15. 2022 High

    Established m6A control of TAB3 expression: METTL3 deposits m6A on TAB3 mRNA and IGF2BP2 reads it to stabilize the transcript, linking the methylation machinery to TAB3-driven renal inflammation.

    Evidence m6A-RIP-seq, RNA-IP, METTL3 conditional-KO mice with knockdown/overexpression

    PMID:35417191

    Open questions at the time
    • Whether m6A-dependent TAB3 induction operates outside renal inflammation untested
  16. 2024 High

    Confirmed in primary macrophages that TAB3 is redundantly required with TAB2 for TLR-induced NF-κB/MAPK activation and IκBζ-dependent IL-6 production, consolidating its role in innate immune cytokine output.

    Evidence TAB2/3 double-deficient bone-marrow-derived macrophages, cytokine ELISA, phosphorylation and IκBζ expression assays

    PMID:38567483

    Open questions at the time
    • TAB3-specific (non-redundant) functions in macrophages not isolated

Open questions

Synthesis pass · forward-looking unresolved questions
  • The signal and machinery that trigger TAB3 dissociation from Beclin 1, and the identity of the TAK1-independent effector that mediates TAB3-driven MAPK activation, remain undefined.
  • No effector kinase identified for TAK1-independent TAB3 MAPK signaling
  • Dissociation trigger for TAB3-Beclin 1 complex unknown
  • No integrated structure of TAB3-TAK1 on polyubiquitin

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 4 GO:0140313 molecular sequestering activity 1
Localization
GO:0005829 cytosol 2
Pathway
R-HSA-162582 Signal Transduction 3 R-HSA-168256 Immune System 3 R-HSA-9612973 Autophagy 2
Partners
BECN1CARD11MAP3K7SMAD7TAB1TRAF2TRAF6USP15
Complex memberships
TAK1-TAB1-TAB3 complex

Evidence

Reading pass · 21 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2004 TAB2 and TAB3 bind preferentially to lysine 63-linked polyubiquitin chains through a conserved zinc finger (ZnF) domain. Mutations of the ZnF domain abolish polyubiquitin binding and the ability to activate TAK1 and IKK. Replacement of the ZnF domain with a heterologous ubiquitin-binding domain restored TAK1 and IKK activation, demonstrating that polyubiquitin binding is essential for signaling. In vitro binding assays, ZnF domain mutagenesis, heterologous domain replacement, IKK activation assays Molecular cell High 15327770
2003 TAB3 physically associates with TAK1 and activates NF-κB. Endogenous TAB3 interacts with TRAF6 in an IL-1-dependent manner and with TRAF2 in a TNF-dependent manner. IL-1 signaling leads to TRAF6-mediated ubiquitination of TAB3. siRNA knockdown of both TAB2 and TAB3 inhibits IL-1- and TNF-induced TAK1 and NF-κB activation, indicating redundant roles. Co-immunoprecipitation, siRNA knockdown, NF-κB reporter assays, ubiquitination assays The EMBO journal High 14633987
2004 TAB3 forms two distinct TAK1 complexes in cells: one containing TAK1-TAB1-TAB2 and another containing TAK1-TAB1-TAB3. Both complexes are activated by TNF-α, IL-1, or LPS. TAB3 electrophoretic mobility decreases upon stimulation and is reversed by protein phosphatase-1, indicating phosphorylation. TAB3 phosphorylation is prevented by the p38 MAPK inhibitor SB203580, indicating TAB3 is phosphorylated via the SAPK2a/p38α pathway. Co-immunoprecipitation, kinase assays, phosphatase treatment, SB203580 inhibitor experiments, p38α-knockout MEFs The Biochemical journal High 14670075
2006 The TAB2/TAB3-binding domain on TAK1 maps to a non-contiguous region within the last C-terminal 100 residues (residues 479–553 necessary and sufficient). Residues 574–693 of TAB2 mediate interaction with TAK1. A GFP-TAK1-C100 fusion protein abolished endogenous TAB2/TAB3 interaction with TAK1, blocked TAK1 phosphorylation, and prevented IKK and MAPK activation by IL-1, TNF, and RANKL, as well as RANKL-induced NFATc1 nuclear accumulation and osteoclast differentiation. Deletion mapping, Co-immunoprecipitation, dominant-negative competition assay, kinase assays, osteoclast differentiation assays The Journal of biological chemistry High 17158449
2009 Crystal structures of TAB2 and TAB3 NZF domains in complex with Lys63-linked diubiquitin resolved at 1.18 Å and 1.40 Å, respectively. Both NZF domains bind the distal ubiquitin via a conserved Thr-Phe dipeptide. A surface specific to TAB2/TAB3 binds the proximal ubiquitin via the Ile44-centered hydrophobic patch. Mutagenesis confirmed both distal and proximal binding sites are required for Lys63-linked diubiquitin binding. X-ray crystallography, site-directed mutagenesis, ubiquitin binding assays The EMBO journal High 19927120
2007 TGF-β-induced Smad7 binds directly to TAB2 and TAB3, blocking recruitment of TAK1 to TRAF2. Formation of Smad7-TAB2 and Smad7-TAB3 complexes suppresses TNF-induced TRAF2-TAB2/TAB3-TAK1 complex assembly. In mouse skin expressing a Smad7 transgene, endogenous TRAF2-TAK1-TAB3 complexes were disrupted and NF-κB nuclear translocation was suppressed. Co-immunoprecipitation, transgenic mouse model, NF-κB nuclear translocation assays Nature immunology High 17384642
2008 TRIM30α, induced by TLR agonists, interacts with the TAB2-TAB3-TAK1 complex and promotes degradation of TAB2 and TAB3, thereby inhibiting NF-κB activation. This constitutes a negative feedback mechanism of TLR signaling. Co-immunoprecipitation, overexpression and transgenic mouse studies, siRNA knockdown, NF-κB activation assays Nature immunology High 18345001
2008 Three IL-1-stimulated phosphorylation sites on TAB3 were identified: Ser60, Thr404, and Ser506. Ser60 and Thr404 are phosphorylated directly by p38α MAPK, while Ser506 is phosphorylated by MAPKAP-K2/K3 (downstream of p38α). TAB1 is required to recruit p38α to the TAK1 complex for TAB3 phosphorylation at Ser60 and Thr404, and to prevent dephosphorylation of TAB3 at Ser506. Mass spectrometry-based phosphosite mapping, TAB1-knockout MEFs, kinase assays with specific inhibitors The Biochemical journal High 18021073
2011 TAB2 and TAB3 constitutively interact with the autophagy mediator Beclin 1 via their coiled-coil domains (CCDs), inhibiting autophagy. Upon autophagy induction, TAB2 and TAB3 dissociate from Beclin 1 and bind TAK1. Overexpression of TAB2/TAB3 suppresses autophagy, while their depletion triggers autophagy. Expression of the C-terminal domain of TAB3 or the CCD of Beclin 1 disrupts this interaction and stimulates autophagy through a pathway requiring endogenous Beclin 1, TAK1, and IKK. Co-immunoprecipitation, domain mapping (CCD), overexpression and siRNA depletion, autophagy readouts (electron microscopy, GFP-LC3 puncta) The EMBO journal High 22081109
2013 TAB2 and TAB3 are essential for B cell activation and B-1/marginal zone B cell development. In B cells lacking both TAB2 and TAB3, MAPK (especially ERK) activation is abolished in response to TLR and CD40 stimulation, whereas NF-κB activation is unaffected. Surprisingly, TAB2/TAB3-mediated MAPK activation in B cells occurs via a pathway independent of TAK1. Conditional double knockout mouse model, B cell stimulation assays, MAPK and NF-κB activation assays, B cell development analysis Journal of immunology High 23509369
2014 Enterovirus 71 3C protease cleaves TAB3 at two sites (Q173-G174 and Q343-G344), requiring 3C protease activity. H40D or C147S substitutions in 3C active sites abolish cleavage. EV71 3C interacts with TAB2 and TAK1, and cleavage of the TAK1/TAB1/TAB2/TAB3 complex inhibits NF-κB activation and cytokine production. Protease activity assays, active-site mutagenesis, Co-immunoprecipitation, NF-κB reporter assays, cleavage site mapping Journal of virology High 24942571
2017 IL-1β can activate the TAB1-TAK1 heterodimer in TAB2/TAB3 double knockout cells, but signaling is transient. TAB2/TAB3 are required for sustained TAK1 activation and for JNK1/2 and p38γ activation. Re-expression of TAB1 or TAB2 (but not an ubiquitin binding-defective mutant of TAB2) restores IL-1β signaling in TAB1/2/3 triple KO cells, establishing that K63-Ub chain binding by TAB2/TAB3 is required for one mode of TAK1 activation. TAB2/TAB3 double KO and TAB1/2/3 triple KO cell lines, re-expression rescue experiments, kinase assays, ubiquitin-binding mutant TAB2 The Biochemical journal High 28507161
2016 TAB3 is O-GlcNAcylated at Ser408 by OGT in triple negative breast cancer cells. This O-GlcNAcylation at Ser408 is required for Thr404 phosphorylation of TAB3, TAK1 activation, and downstream NF-κB activation. O-GlcNAcylation of TAB3 is induced by p38 MAPK and in turn enhances TAK1-mediated p38 MAPK activation, forming a positive feedback loop. O-GlcNAc site mapping (Ser408), site-directed mutagenesis, OGT co-expression, kinase activation assays Oncotarget Medium 27009840
2019 Multiple GPCR agonists (thrombin, histamine, PGE2, ADP) activate p38 MAPK via a non-canonical TAB1-TAB3-dependent pathway in primary human endothelial cells (HUVECs), bypassing canonical MKK3/MKK6 upstream kinases. TAB3 expression is confirmed in endothelial cells, and thrombin-induced p38 activation in HDMECs specifically depends on TAB1-TAB3 (not TAB1-TAB2). IL-6 production required both TAB1-TAB2 and TAB1-TAB3. siRNA knockdown, p38 and MKK3/6 phosphorylation assays, IL-6 ELISA, multiple endothelial cell types The Journal of biological chemistry Medium 30760523
2020 USP15 stabilizes TAB3 by inhibiting NBR1-mediated selective autophagic degradation of TAB3, independent of USP15's deubiquitinating activity. This TAB3 stabilization potentiates NF-κB activation downstream of TNFα and IL-1β. Co-immunoprecipitation, ubiquitination assays, lysosome inhibitor experiments, siRNA knockdown, NF-κB reporter assays The FEBS journal Medium 31903660
2022 METTL3 promotes m6A modification of TAB3 mRNA at its stop codon region. IGF2BP2 reads this m6A modification and stabilizes TAB3 mRNA. METTL3 knockdown reduces TAB3 protein levels and attenuates renal inflammation; METTL3 overexpression increases TAB3 stability and promotes inflammation. This mechanism was validated in vitro and in conditional METTL3 knockout mouse models. m6A-RIP sequencing, RNA-IP (IGF2BP2 pulldown), METTL3 conditional knockout mice, siRNA knockdown and overexpression Science translational medicine High 35417191
2016 TAB2 and TAB3 connect signaling molecules to activate IKK in B-cell receptor (BCR) signaling by linking TAK1 to CARMA1. Loss of TAB2 and TAB3 abolished BCR-induced IKK activation and TAK1 association with CARMA1. Deletion of TAB3 domains (ubiquitin-conjugation-to-ER degradation domain, coiled-coil domain, and zinc finger domain) each blocked IKK activation and CARMA1 association. TAB2/TAB3-deficient DT40 B cell lines, domain deletion mutants, Co-immunoprecipitation, IKK activation assays FEBS letters Medium 27497262
2020 TAB3 promotes STAT3 phosphorylation through formation of a TAB3-TAK1-STAT3 complex, leading to upregulation of PIM1 expression and colorectal cancer proliferation. TAB3 knockdown decreased STAT3 phosphorylation and PIM1 expression; PIM1 overexpression rescued proliferation defects caused by TAB3 knockdown. Co-immunoprecipitation, siRNA knockdown, rescue overexpression experiments, xenograft tumor assays, immunoblotting Experimental cell research Medium 32229191
2024 TAB2 and TAB3 are redundantly required in macrophages for TLR-induced NF-κB and MAPK activation and pro-inflammatory cytokine/chemokine production. Double deficiency of TAB2 and TAB3 severely impairs IκBζ expression at mRNA and protein levels, thereby impairing IL-6 production in response to LPS or Pam3CSK4. TAB2/TAB3 double-deficient bone marrow-derived macrophages, cytokine ELISA, NF-κB and MAPK phosphorylation assays, IκBζ expression analysis International immunology High 38567483
2002 TAB3 was identified in Xenopus laevis as a novel TAK1-binding protein with a role in regulating TAK1 activity during neural induction, with a proposed model of BMP inhibition partly through TAK1 regulation. Xenopus cDNA microarray, gain-of-function studies in ectodermal explants Development (Cambridge, England) Low 12403722
2017 TAB3 regulates Survivin expression by activating the NF-κB pathway through formation of a TAK1-TAB3-TRAF6 complex. TAB3 knockdown decreased Survivin expression and suppressed colorectal cancer cell migration and invasion in vitro and liver metastasis in vivo. Co-immunoprecipitation (TAK1-TAB3-TRAF6 complex), siRNA knockdown, invasion/migration assays, in vivo liver metastasis model Oncotarget Medium 29290971

Source papers

Stage 0 corpus · 48 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2004 TAB2 and TAB3 activate the NF-kappaB pathway through binding to polyubiquitin chains. Molecular cell 749 15327770
2012 The microRNA miR-23b suppresses IL-17-associated autoimmune inflammation by targeting TAB2, TAB3 and IKK-α. Nature medicine 372 22660635
2022 Inhibition of METTL3 attenuates renal injury and inflammation by alleviating TAB3 m6A modifications via IGF2BP2-dependent mechanisms. Science translational medicine 262 35417191
2003 Role of the TAB2-related protein TAB3 in IL-1 and TNF signaling. The EMBO journal 239 14633987
2008 TRIM30 alpha negatively regulates TLR-mediated NF-kappa B activation by targeting TAB2 and TAB3 for degradation. Nature immunology 215 18345001
2014 MicroRNA-26b suppresses the NF-κB signaling and enhances the chemosensitivity of hepatocellular carcinoma cells by targeting TAK1 and TAB3. Molecular cancer 145 24565101
2004 TAB3, a new binding partner of the protein kinase TAK1. The Biochemical journal 143 14670075
2007 Smad7 binds to the adaptors TAB2 and TAB3 to block recruitment of the kinase TAK1 to the adaptor TRAF2. Nature immunology 123 17384642
2009 Structural basis for specific recognition of Lys 63-linked polyubiquitin chains by NZF domains of TAB2 and TAB3. The EMBO journal 121 19927120
2006 TAK1-dependent signaling requires functional interaction with TAB2/TAB3. The Journal of biological chemistry 120 17158449
2013 Genome-wide screening reveals that miR-195 targets the TNF-α/NF-κB pathway by down-regulating IκB kinase alpha and TAB3 in hepatocellular carcinoma. Hepatology (Baltimore, Md.) 111 23487264
2014 Enterovirus 71 3C inhibits cytokine expression through cleavage of the TAK1/TAB1/TAB2/TAB3 complex. Journal of virology 86 24942571
2011 Inhibition of autophagy by TAB2 and TAB3. The EMBO journal 84 22081109
2004 Identification of a human NF-kappaB-activating protein, TAB3. Proceedings of the National Academy of Sciences of the United States of America 72 14766965
2020 USP15 potentiates NF-κB activation by differentially stabilizing TAB2 and TAB3. The FEBS journal 60 31903660
2015 Human MicroRNA miR-532-5p Exhibits Antiviral Activity against West Nile Virus via Suppression of Host Genes SESTD1 and TAB3 Required for Virus Replication. Journal of virology 60 26676784
2008 Roles for TAB1 in regulating the IL-1-dependent phosphorylation of the TAB3 regulatory subunit and activity of the TAK1 complex. The Biochemical journal 60 18021073
2012 TGF-β-associated miR-27a inhibits dendritic cell-mediated differentiation of Th1 and Th17 cells by TAB3, p38 MAPK, MAP2K4 and MAP2K7. Genes and immunity 54 23034448
2013 Essential roles of K63-linked polyubiquitin-binding proteins TAB2 and TAB3 in B cell activation via MAPKs. Journal of immunology (Baltimore, Md. : 1950) 52 23509369
2002 Gene profiling during neural induction in Xenopus laevis: regulation of BMP signaling by post-transcriptional mechanisms and TAB3, a novel TAK1-binding protein. Development (Cambridge, England) 48 12403722
2019 G protein-coupled receptors activate p38 MAPK via a non-canonical TAB1-TAB2- and TAB1-TAB3-dependent pathway in endothelial cells. The Journal of biological chemistry 42 30760523
2017 Interleukin-1 and TRAF6-dependent activation of TAK1 in the absence of TAB2 and TAB3. The Biochemical journal 37 28507161
2017 Paclitaxel alleviated liver injury of septic mice by alleviating inflammatory response via microRNA-27a/TAB3/NF-κB signaling pathway. Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie 34 29156532
2023 Macrophage-derived exosomes modulate wear particle-induced osteolysis via miR-3470b targeting TAB3/NF-κB signaling. Bioactive materials 32 36911207
2016 TAB3 O-GlcNAcylation promotes metastasis of triple negative breast cancer. Oncotarget 31 27009840
2015 MiR-30a attenuates immunosuppressive functions of IL-1β-elicited mesenchymal stem cells via targeting TAB3. FEBS letters 29 26555189
2016 Interleukin-17A inhibits cell autophagy under starvation and promotes cell migration via TAB2/TAB3-p38 mitogen-activated protein kinase pathways in hepatocellular carcinoma. European review for medical and pharmacological sciences 26 26875893
2023 Efficient proteome-wide identification of transcription factors targeting Glu-1: A case study for functional validation of TaB3-2A1 in wheat. Plant biotechnology journal 20 37381172
2022 miR-23b/TAB3/NF-κB/p53 axis is involved in hippocampus injury induced by cerebral ischemia-reperfusion in rats: The protective effect of chlorogenic acid. BioFactors (Oxford, England) 19 35201648
2020 Stabilization of the TAK1 adaptor proteins TAB2 and TAB3 is critical for optimal NF-κB activation. The FEBS journal 19 31997570
2015 TAB3 involves in hepatic insulin resistance through activation of MAPK pathway. General and comparative endocrinology 17 26320856
2020 TAB3 upregulates PIM1 expression by directly activating the TAK1-STAT3 complex to promote colorectal cancer growth. Experimental cell research 14 32229191
2020 LncRNA NEAT1 regulated inflammation and apoptosis in a rat model of sepsis-induced acute kidney injury via MiR-27a-3p/TAB3 axis. Bioscience, biotechnology, and biochemistry 13 32698679
2015 TAB3 overexpression promotes cell proliferation in non-small cell lung cancer and mediates chemoresistance to CDDP in A549 cells via the NF-κB pathway. Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine 13 26476534
2016 Loss of TAB3 expression by shRNA exhibits suppressive bioactivity and increased chemical sensitivity of ovarian cancer cell lines via the NF-κB pathway. Cell proliferation 12 27651027
2011 Rhesus monkey TRIM5α represses HIV-1 LTR promoter activity by negatively regulating TAK1/TAB1/TAB2/TAB3-complex-mediated NF-κB activation. Archives of virology 12 21918865
2018 MicroRNA-16 inhibits the lipopolysaccharide-induced inflammatory response in nucleus pulposus cells of the intervertebral disc by targeting TAB3. Archives of medical science : AMS 10 33747285
2017 TAB3 upregulates Survivin expression to promote colorectal cancer invasion and metastasis by binding to the TAK1-TRAF6 complex. Oncotarget 10 29290971
2018 TAB3 promotes human esophageal squamous cell carcinoma proliferation and invasion via the NF‑κB pathway. Oncology reports 9 30226617
2018 MicroRNA-23b attenuates the H2O2-induced injury of microglial cells via TAB3/NF-κB signaling pathway. International journal of clinical and experimental pathology 9 31949662
2021 LncRNA PCIR Is an Oncogenic Driver via Strengthen the Binding of TAB3 and PABPC4 in Triple Negative Breast Cancer. Frontiers in oncology 8 34012913
2016 TAK1 adaptor proteins, TAB2 and TAB3, link the signalosome to B-cell receptor-induced IKK activation. FEBS letters 8 27497262
2024 TAK1-binding protein 2 (TAB2) and TAB3 are redundantly required for TLR-induced cytokine production in macrophages. International immunology 5 38567483
2020 ZEB2-AS1 regulates the expression of TAB3 and promotes the development of colon cancer by adsorbing microRNA-188. European review for medical and pharmacological sciences 5 32373954
2020 TAB3 overexpression promotes NF-κB activation and inflammation in acute pancreatitis. American journal of blood research 5 32923091
2023 miR‑27a‑3p upregulation by p65 facilitates cervical tumorigenesis by increasing TAB3 expression and is involved in the positive feedback loop of NF‑κB signaling. Oncology reports 4 37203408
2016 Up-Regulation of TAB3 Is Involved in Neuronal Apoptosis After Intracerebral Hemorrhage. Cellular and molecular neurobiology 4 27352012
2017 TAB3 defect induces augmented cardioprotection loss from ischemic injury. Cell biology international 1 28462515

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