Affinage

AJUBA

LIM domain-containing protein ajuba · UniProt Q96IF1

Length
538 aa
Mass
56.9 kDa
Annotated
2026-06-09
87 papers in source corpus 50 papers cited in narrative 50 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

AJUBA is a cytoplasm-to-nucleus shuttling LIM-domain scaffold that integrates mechanical and growth-factor signals at adherens junctions, the mitotic apparatus, and the nucleus to control cell proliferation, adhesion, and gene expression (PMID:12417594, PMID:20303269). At cell-cell contacts, AJUBA is recruited to cadherin complexes through α-catenin and binds F-actin, stabilizing junctions under tension (PMID:12417594, PMID:30006462); this α-catenin association is itself tension-dependent and constitutes the mechanotransduction step that controls junctional AJUBA loading (PMID:24995985, PMID:30659113). Junctional AJUBA negatively regulates the Hippo pathway: it binds and sequesters the LATS/Warts–WW45/Sav kinase module to inhibit phosphorylation of YAP/Yorkie, an activity conserved from Drosophila to mammals and tuned by cytoskeletal tension (PMID:20303269, PMID:24995985, PMID:27457617). EGFR-RAS-MAPK and JNK signaling phosphorylate AJUBA-family proteins to enhance their LATS binding, integrating receptor and stress inputs into Hippo output (PMID:23484853, PMID:24023255). At the centrosome and kinetochore, AJUBA activates Aurora-A by relieving its autoinhibitory N/C-terminal interaction and driving autophosphorylation, committing cells to mitosis (PMID:13678582, PMID:24680704). In the nucleus, AJUBA acts as a transcriptional corepressor for SNAG-domain factors Snail and Gfi1 by recruiting PRMT5 and HDAC activity to repress targets including E-cadherin (PMID:17909014, PMID:18347060, PMID:18805794), and as a ligand-dependent corepressor for retinoic acid receptors (PMID:20133701), while serving as an obligate p300/CBP-recruiting coactivator for PPARγ, C/EBPβ, SP1, and Twist to drive adipogenic and pro-migratory programs (PMID:26113042, PMID:34619292, PMID:31101117, PMID:34173718). AJUBA also drives cell migration by activating PIPKIα to position PI(4,5)P2 synthesis at lamellipodia and by localizing p130Cas to nascent focal complexes to promote Rac activation (PMID:15728191, PMID:15870270, PMID:22105346). AJUBA stability is set by competing modifications: GSK-3β-primed phosphorylation of a degron recruits SCFβ-TrCP for ubiquitination (PMID:40367710), Hakai induces its neddylation (PMID:30041665), and USP7 deubiquitination stabilizes it (PMID:39522755).

Mechanistic history

Synthesis pass · year-by-year structured walk · 23 steps
  1. 1999 High

    Established AJUBA as a positive regulator of MAP kinase signaling, linking it to Grb2/Ras and proliferative control before any structural role was known.

    Evidence In vitro and in vivo Grb2 binding, MAPK activity assay, and Xenopus oocyte maturation with Grb2/Ras epistasis

    PMID:10330178

    Open questions at the time
    • Direct mechanism by which Grb2 binding amplifies MAPK output not defined
    • No structural basis for the proline-rich/SH3 interaction
  2. 2000 Medium

    Showed AJUBA shuttles between cytoplasm and nucleus via an NES and that its LIM domains exert distinct effects on proliferation versus differentiation, framing it as a context-switching factor.

    Evidence NES mutagenesis, nuclear accumulation, and proliferation/differentiation assays in P19 cells with JNK readout

    PMID:11029037

    Open questions at the time
    • Nuclear targets driving differentiation not identified
    • Mechanism of JNK requirement unresolved
  3. 2002 High

    Defined AJUBA as a junctional adaptor bound to α-catenin and F-actin, providing the structural basis for its later mechanotransduction roles.

    Evidence Reciprocal co-IP, immunofluorescence, F-actin binding, and Ajuba-null mouse keratinocyte junction phenotype

    PMID:12417594

    Open questions at the time
    • Whether junctional AJUBA signals to a specific downstream pathway not addressed at this stage
    • Direct vs indirect α-catenin contact not mapped
  4. 2003 High

    Identified AJUBA as an Aurora-A activator required for mitotic commitment, assigning it a direct role in cell-cycle entry.

    Evidence Yeast two-hybrid, co-IP, in vitro kinase activation assay, and RNAi in synchronized HeLa cells

    PMID:13678582

    Open questions at the time
    • How junctional/nuclear pools relate to the centrosomal Aurora-A pool unclear
    • Whether activation is direct allosteric or substrate-priming not resolved here
  5. 2005 High

    Connected AJUBA to cell migration machinery through p130Cas/Rac and through PIPKIα-mediated PI(4,5)P2 production, establishing a cytoskeletal/lipid signaling axis.

    Evidence Ajuba-null MEF migration, FRET Rac activation, rescue, and in vitro PIPKIα enzyme assay with lipid quantification

    PMID:15728191 PMID:15870270

    Open questions at the time
    • How AJUBA spatially couples p130Cas localization to PI(4,5)P2 synthesis not integrated
    • Direct vs scaffolded activation of PIPKIα at lamellipodia
  6. 2005 High

    Placed AJUBA in IL-1/NF-κB signaling as an organizer of the PKCζ/p62/TRAF6 complex, broadening its adaptor role to innate signaling.

    Evidence Yeast two-hybrid, co-IP, in vitro PKCζ kinase assay, and NF-κB reporter in Ajuba-null MEFs

    PMID:15870274

    Open questions at the time
    • In vivo relevance to inflammatory responses not tested
    • Relationship to later p62-mediated AJUBA degradation not connected
  7. 2007 High

    Defined AJUBA as a SNAG-domain corepressor and a negative Wnt regulator, establishing its nuclear transcriptional and signaling-suppressor functions.

    Evidence Yeast two-hybrid, ChIP at endogenous promoters, reporter assays for SNAG factors; co-IP and β-catenin stability assays for Wnt

    PMID:17621269 PMID:17909014

    Open questions at the time
    • Corepressor enzymatic effectors not yet identified (resolved later)
    • Mechanism of Wnt-induced AJUBA destabilization undefined at this stage
  8. 2008 High

    Identified the enzymatic effectors of AJUBA repression—PRMT5 and HDAC—showing it recruits histone-modifying activities to silence targets like E-cadherin.

    Evidence Co-IP, gel filtration, HDAC and histone arginine methylation assays, ChIP at endogenous loci

    PMID:18347060 PMID:18805794

    Open questions at the time
    • Selectivity determinants for PRMT5 vs HDAC recruitment not mapped
    • Whether the same complex operates at all SNAG targets unknown
  9. 2009 Medium

    Extended AJUBA's mitotic role beyond Aurora-A activation to microtubule-dependent localization at centrosomes and kinetochores with Aurora B and BUBR1.

    Evidence Mitotic immunofluorescence, in vitro microtubule binding, microtubule regrowth, and co-IP with Aurora B/BUBR1

    PMID:18710370

    Open questions at the time
    • Functional consequence of Aurora B/BUBR1 binding not dissected
    • Single lab
  10. 2010 High

    Established the conserved AJUBA-family role as negative Hippo regulators that inhibit LATS/Warts to activate YAP/Yorkie, anchoring its growth-control function.

    Evidence Drosophila genetic epistasis, co-IP in two species, YAP/Yki phosphorylation assays

    PMID:20303269

    Open questions at the time
    • Subcellular site of LATS inhibition not yet specified (clarified later)
    • How mechanical inputs feed in not addressed here
  11. 2010 Medium

    Broadened AJUBA's functional repertoire to RNA silencing (P-body/miRNA machinery), nuclear receptor corepression of RAR/RXR, and ciliogenesis/left-right asymmetry.

    Evidence Co-IP with RISC/decapping factors and m7GTP pull-down; ligand-dependent RAR co-IP with ChIP; medaka morpholino ciliogenesis and laterality assays

    PMID:20133701 PMID:20457130 PMID:20616046

    Open questions at the time
    • miRNA-silencing role not integrated with adaptor functions
    • Ciliogenesis mechanism downstream of basal-body localization unknown
  12. 2011 High

    Refined the Aurora-A relationship in vivo, showing the Drosophila ortholog maintains centrosomal Aurora-A localization rather than activating kinase activity, and identified a Rac-PAK1-AJUBA junctional feedback loop.

    Evidence Drosophila jub mutant Aurora-A localization/activity readouts; in vitro PAK1 phosphorylation of AJUBA at Thr172, phosphomimetic rescue, and Rac-GTP pull-down

    PMID:21402878 PMID:22105346

    Open questions at the time
    • Activation vs maintenance models of Aurora-A regulation not reconciled across systems
    • How PAK1 phosphorylation alters Rac-binding preference structurally unknown
  13. 2013 High

    Wired growth-factor and stress kinases into Hippo control by showing EGFR-RAS-MAPK and JNK phosphorylate AJUBA-family proteins to enhance LATS binding.

    Evidence Drosophila epistasis (EGFR/Ras/jub), MAPK- and JNK-promoted co-IP, and in vitro JNK phosphorylation of LIMD1

    PMID:23484853 PMID:24023255

    Open questions at the time
    • Specific AJUBA phospho-sites engaged by MAPK not all mapped
    • Quantitative contribution of each kinase to YAP output unresolved
  14. 2013 Medium

    Tied AJUBA's Hippo suppression to a cancer context and to genome-integrity surveillance, expanding its disease relevance.

    Evidence LATS2-dependent YAP suppression in mesothelioma (reporter + siRNA rescue); RPA association with ATR/Chk1 pathway readouts on depletion

    PMID:23755068 PMID:24336325

    Open questions at the time
    • Direct vs indirect RPA engagement unresolved at this stage (addressed later)
    • Single-lab observations
  15. 2014 High

    Established the mechanotransduction logic: cytoskeletal tension promotes AJUBA-α-catenin association and tension-dependent Warts recruitment to junctions, converting mechanical force into growth signals.

    Evidence Drosophila myosin/Jub/Warts epistasis, co-IP, tension-dependent junctional imaging, and wing growth quantification; plus domain-mapped Aurora-A activation by in vitro kinase assay

    PMID:24680704 PMID:24995985

    Open questions at the time
    • Molecular sensor within α-catenin not yet localized (resolved 2019)
    • How tension-released LATS reactivates not detailed
  16. 2016 High

    Resolved where AJUBA inhibits Hippo (cytosolic sequestration of an inhibited LATS complex) and identified CDK1 phosphorylation as a Hippo-independent driver of proliferation, plus a JAK1/STAT1 survival mechanism.

    Evidence Cytosolic-fraction co-IP and YAP readouts in proliferating vs arrested cells; in vitro CDK1 kinase assay with S119A/S175A mutants and xenografts; AJUBA-JAK1 FERM co-IP with STAT1/IFIT2 readouts

    PMID:27226586 PMID:27457617 PMID:27893714

    Open questions at the time
    • Reconciliation of cytosolic-only model with junctional mechanotransduction model unresolved
    • How CDK1 sites alter AJUBA function mechanistically unclear
  17. 2018 Medium

    Provided structural and regulatory detail on AJUBA functions: direct RPA70 binding restraining ATR, force-sensitive junctional localization domains, and Hakai-induced neddylation controlling stability.

    Evidence Direct Ajuba-RPA70 binding and cell-cycle regulation; live imaging with domain truncations in Drosophila embryos; Hakai HYB-domain co-IP and neddylation assay with inhibitor controls

    PMID:29934626 PMID:30006462 PMID:30041665

    Open questions at the time
    • Physiological trigger switching AJUBA from junction-stabilizing to mitotic/nuclear pools unclear
    • Neddylation functional consequence beyond stability undefined
  18. 2019 Medium

    Pinpointed α-catenin as the tension mechanotransducer recruiting Jub and added SP1 as a coactivator partner in a feed-forward loop, deepening both mechanical and transcriptional models.

    Evidence Domain-deletion α-catenin co-IP with constitutive Jub recruitment and Yorkie/wing readouts; SP1 GST pull-down, co-IP, and ChIP

    PMID:30659113 PMID:31101117

    Open questions at the time
    • Structural conformational change in α-catenin transmitting force not defined
    • Single-lab observations
  19. 2015 High

    Defined AJUBA as an obligate p300/CBP-recruiting coactivator for adipogenic transcription factors, contrasting with its corepressor roles and establishing context-dependent cofactor switching.

    Evidence Domain-mapped co-IP (PPARγ, p300/CBP), ChIP with histone acetylation, and 3T3-L1 adipogenesis assays (extended to C/EBPβ in 2021 and Twist in 2017)

    PMID:26113042 PMID:34173718 PMID:34619292

    Open questions at the time
    • What determines corepressor vs coactivator outcome at a given promoter unknown
    • In vivo adipogenic requirement not established
  20. 2021 High

    Revealed AJUBA's role in PINK1-dependent mitophagy and antiviral defense, and identified p62/autophagy as a degradative regulator of AJUBA.

    Evidence ZIKV NS5-Ajuba co-IP, live imaging of mitochondrial translocation, Ajuba-knockout mouse infection model; p62 UBA-dependent NF-κB and autophagic degradation assays

    PMID:34706234 PMID:34735553

    Open questions at the time
    • How AJUBA activates PINK1 mechanistically not defined
    • Link between mitophagy and nuclear/junctional pools unexplored
  21. 2023 Medium

    Extended AJUBA function to Golgi ribbon shaping via a PRMT5/Aurora-A/HURP module, to p53 turnover via MDM2, and to nephrocyte slit-diaphragm Hippo feedback, illustrating its breadth of scaffolded enzymatic complexes.

    Evidence Ajuba-PRMT5-Aurora-A complex co-IP with HURP modification/rescue; Ajuba-p53-MDM2 co-IP with protein/mRNA dissociation; Drosophila nephrocyte epistasis and permeability assays

    PMID:36930055 PMID:36931700 PMID:37370099

    Open questions at the time
    • Whether the Golgi PRMT5/Aurora-A complex overlaps the nuclear repression complex unknown
    • Single-lab findings each
  22. 2024 Medium

    Established a stability-control network for AJUBA: USP7 deubiquitination stabilizes it and supports cell-cell adhesion, while GSK-3β-primed SCFβ-TrCP ubiquitination degrades it.

    Evidence USP7-Ajuba co-IP with quantitative proteomics and FT671 inhibitor; in vitro GSK3β kinase assay, S163A degron mutagenesis, β-TrCP WD40 co-IP, and ubiquitination assay

    PMID:39522755 PMID:40367710

    Open questions at the time
    • Signals controlling GSK-3β-mediated degron phosphorylation in different contexts unclear
    • Interplay between neddylation, ubiquitination, and USP7 deubiquitination not integrated
  23. 2025 Medium

    Refined Hippo regulation mechanistically, showing Jub promotes Warts N-terminal phosphorylation and recruits Warts into biomolecular condensates that tune kinase activity.

    Evidence Condensate imaging, Warts N-terminal phospho-site mutagenesis, and Drosophila genetics identifying Minibrain and HIPK as kinases

    PMID:41351836

    Open questions at the time
    • Whether mammalian AJUBA/LATS form analogous condensates untested
    • How condensation switches between LATS inhibition and activation unresolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • How AJUBA's many activities—junctional mechanotransduction, mitotic Aurora-A regulation, opposing transcriptional cofactor roles, mitophagy, and Hippo/Wnt/YAP control—are partitioned spatially and temporally within a single cell remains the central unresolved question.
  • No structural model explaining how the same LIM domains select among Aurora-A, LATS, α-catenin, and transcription-factor partners
  • The signal that switches AJUBA between corepressor and coactivator states is unknown
  • Reconciliation of tension-dependent junctional vs cytosolic-sequestration models of Hippo inhibition is incomplete

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140110 transcription regulator activity 8 GO:0060090 molecular adaptor activity 5 GO:0098772 molecular function regulator activity 4 GO:0008092 cytoskeletal protein binding 2 GO:0042393 histone binding 2
Localization
GO:0005634 nucleus 4 GO:0005886 plasma membrane 4 GO:0005815 microtubule organizing center 3 GO:0005829 cytosol 2 GO:0005694 chromosome 1
Pathway
R-HSA-162582 Signal Transduction 5 R-HSA-392499 Metabolism of proteins 4 R-HSA-74160 Gene expression (Transcription) 4 R-HSA-1640170 Cell Cycle 3 R-HSA-168256 Immune System 2
Partners
AURKABTRCCTNNA1LATS2PRMT5RPA70TRAF6YAP1
Complex memberships
Ajuba/PRMT5/Aurora-A complexLATS/Warts-WW45/Sav Hippo kinase complexPKCζ/p62/TRAF6 signaling complexSNAIL/AJUBA/PRMT5 corepressor complex

Evidence

Reading pass · 50 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2003 Ajuba is an activator of Aurora-A kinase required for mitotic commitment: Ajuba and Aurora-A interact in mitotic cells and become phosphorylated; in vitro, Ajuba induces autophosphorylation and consequent activation of Aurora-A. Depletion of Ajuba prevented Aurora-A activation at centrosomes in late G2 phase and inhibited mitotic entry. Yeast two-hybrid screen (binding partner identification), co-immunoprecipitation, in vitro kinase assay, RNA interference in synchronized HeLa cells Cell High 13678582
1999 Ajuba specifically associates with Grb2 through its N-terminal proline-rich pre-LIM domain interacting with either SH3 domain of Grb2; Ajuba augments MAP kinase activity in fibroblasts and promotes Xenopus oocyte meiotic maturation in a Grb2- and Ras-dependent manner. In vitro binding assay, co-immunoprecipitation in vivo, MAP kinase activity assay, Xenopus oocyte meiotic maturation assay Molecular and cellular biology High 10330178
2000 Ajuba contains a functional nuclear export signal and shuttles into the nucleus; accumulation of Ajuba LIM domains in the nucleus of P19 embryonal cells causes growth inhibition and spontaneous endodermal differentiation. The differentiating effect maps to LIM domain 3, proliferation regulation to LIM domains 1 and 2. Ajuba-induced differentiation requires c-Jun kinase activation. Nuclear export signal mutagenesis, nuclear accumulation assay, cell proliferation and differentiation assays in P19 cells, c-Jun kinase activity assay Molecular biology of the cell Medium 11029037
2002 Ajuba is recruited to cadherin-dependent cell-cell adhesive complexes in a regulated manner; Ajuba interacts with α-catenin at adherens junctions, α-catenin is required for efficient Ajuba recruitment to junctions, and Ajuba interacts directly with F-actin. Keratinocytes from Ajuba null mice show abnormal cell-cell junction formation and/or stability. Co-immunoprecipitation, immunofluorescence localization, knockout mouse keratinocytes, F-actin binding assay The Journal of biological chemistry High 12417594
2002 Ajuba interacts with the amino terminus of the glial glutamate transporter GLT-1; Ajuba is coimmunoprecipitated with GLT-1 from brain and co-localizes with GLT-1 at the plasma membrane when co-expressed. Ajuba co-expression did not affect GLT-1 Km or Vmax for glutamate. Co-immunoprecipitation from brain tissue, co-expression in COS cells with co-localization Molecular and cellular neurosciences Medium 11860269
2005 Ajuba promotes cell migration by localizing p130Cas to nascent focal complexes: Ajuba associates with the focal adhesion-targeting domain of p130Cas and is required for tyrosine phosphorylation of FAK, p130Cas, Crk, and Dock180 at nascent focal complexes. Rac activation is blunted in Ajuba null cells; Ajuba acts upstream of p130Cas for Rac activation. Ajuba null mouse embryonic fibroblast migration assay, co-immunoprecipitation, FRET-based Rac activation assay, rescue experiments The Journal of cell biology High 15728191
2005 Ajuba regulates cellular PI(4,5)P2 levels by interacting with and activating PIPKIα (PI(4)P 5-kinase) activity while inhibiting PIPKIIβ. In Ajuba-null MEFs, PI(4,5)P2 levels are decreased with a corresponding increase in PI(4)P. Localization of PI(4,5)P2 synthesis to lamellipodia in migrating cells requires Ajuba. In vitro PIPKIα enzymatic activity assay with recombinant Ajuba, lipid phosphoinositide quantification in Ajuba-null MEFs, immunofluorescence localization Molecular and cellular biology High 15870270
2005 Ajuba modulates IL-1-induced NF-κB activation by influencing the assembly and activity of the PKCζ/p62/TRAF6 signaling complex: Ajuba interacts with p62, TRAF6, and PKCζ; recruits TRAF6 to p62; activates PKCζ in vitro; and is a PKCζ substrate. Ajuba null MEFs are defective in NF-κB activation and IKK activity following IL-1 stimulation. Yeast two-hybrid screen, co-immunoprecipitation, in vitro PKCζ kinase assay, Ajuba null mouse embryonic fibroblasts NF-κB reporter assay Molecular and cellular biology High 15870274
2006 Ajuba forms a complex with LATS2 during mitosis; LATS2 contributes to mitotic phosphorylation of Ajuba. Depletion of either LATS2 or Ajuba impairs centrosomal accumulation of γ-tubulin and spindle formation at the onset of mitosis. Yeast two-hybrid screening, co-immunoprecipitation, RNAi depletion, immunofluorescence of γ-tubulin at centrosomes FEBS letters Medium 16413547
2007 Ajuba functions as a corepressor for SNAG domain-containing transcription factors (Snail, Gfi1): Ajuba interacts with the SNAG domain in vitro and in vivo, co-localizes with it, and enhances SNAG-mediated transcriptional repression. Chromatin immunoprecipitation shows SNAG-dependent assembly of a multiprotein repression complex including Ajuba at target promoters with histone modifications consistent with repression. Yeast two-hybrid, co-immunoprecipitation, integrated reporter gene assay, chromatin immunoprecipitation (ChIP), nucleocytoplasmic shuttling assay Cancer research High 17909014
2007 Ajuba negatively regulates Wnt signaling by promoting GSK-3β-mediated phosphorylation of β-catenin: enforced Ajuba expression destabilizes β-catenin and suppresses Wnt target gene expression; Ajuba reinforces the association between β-catenin and GSK-3β. Wnt stimulation induces β-catenin accumulation and destabilization of Ajuba. Overexpression and knockdown in cells, co-immunoprecipitation, Western blot for β-catenin stability, luciferase reporter assay for Wnt target genes Oncogene Medium 17621269
2008 Ajuba recruits PRMT5 to the SNAIL/AJUBA corepressor complex at the E-cadherin promoter: PRMT5 binds the non-LIM region of Ajuba, is translocated into the nucleus in a SNAIL- and AJUBA-dependent manner, and the ternary SNAIL/AJUBA/PRMT5 complex mediates arginine methylation of histones at the E-cadherin locus causing its repression. Co-immunoprecipitation, ChIP at E-cadherin promoter, histone arginine methylation assay, RNAi depletion, luciferase reporter assay Molecular and cellular biology High 18347060
2008 Ajuba forms an endogenous complex with Gfi1 and HDAC and functions as a corepressor for Gfi1 autoregulation in a histone deacetylase-dependent manner: active HDAC activity co-immunoprecipitates with Ajuba or Gfi1; Ajuba LIM domains directly bind Gfi1; ChIP and reciprocal knockdown show selective Ajuba co-repressor function at Gfi1 target genes. Co-immunoprecipitation, gel filtration, HDAC activity assay, ChIP, reciprocal knockdown, reporter assay The Journal of biological chemistry High 18805794
2009 Ajuba localizes to centrosomes and kinetochores during mitosis in a microtubule-dependent manner; Ajuba binds microtubules in vitro and follows nascent microtubules from centrosomes to kinetochores. Ajuba interacts with Aurora B and BUBR1 at kinetochores; BUBR1 siRNA disrupts chromosome alignment and modifies Ajuba localization due to premature mitotic exit. Immunofluorescence during mitosis, in vitro microtubule binding assay, microtubule regrowth assay, co-immunoprecipitation with Aurora B and BUBR1, siRNA knockdown Biology of the cell Medium 18710370
2010 Ajuba LIM proteins (Ajuba, LIMD1, WTIP) are negative regulators of the Hippo pathway: in Drosophila, the single ortholog djub is required for normal epithelial organ size; epistasis places djub downstream of hpo. In mammalian and Drosophila cells, Ajuba LIM proteins/dJub interact with LATS/Warts and WW45/Sav to inhibit phosphorylation of YAP/Yki. Drosophila genetic knockout and RNAi, epistasis analysis (double mutant), co-immunoprecipitation in mammalian and Drosophila cells, YAP/Yki phosphorylation assay Current biology : CB High 20303269
2010 Ajuba LIM proteins (LIMD1, Ajuba, WTIP) are required for miRNA-mediated but not siRNA-mediated gene silencing; they localize to P-bodies and bind Ago1/2, RCK, Dcp2, and eIF4E in vivo; they also bind the mRNA 5' m7GTP cap-protein complex, and their interaction with eIF4E prevents 4EBP1 and eIF4G interaction. Co-immunoprecipitation with Ago1/2, RCK, Dcp2, eIF4E; m7GTP cap pull-down; RNAi knockdown with miRNA reporter assay; P-body localization by immunofluorescence Proceedings of the National Academy of Sciences of the United States of America Medium 20616046
2010 Ajuba functions as a nuclear receptor corepressor for a subset of nuclear hormone receptors: Ajuba selectively interacts with RARs and RXRs in a ligand-dependent manner through CoRNR-like motifs; simultaneous mutation of these motifs abolishes RAR binding and repression; Ajuba occupies RARE control elements in the absence of atRA and dissociates upon atRA stimulation; PRMT5 binding to Ajuba is mutually exclusive with RAR binding. Co-immunoprecipitation (ligand-dependent), mutagenesis of nuclear receptor interacting motifs, ChIP at endogenous RAR target genes, RARE reporter assay, RNAi depletion in P19 cells Proceedings of the National Academy of Sciences of the United States of America High 20133701
2011 In Drosophila neuroblasts, Jub (Ajuba ortholog) is required to maintain Aurora-A at the centrosome but does not activate Aurora-A kinase activity itself; in jub mutants Aurora-A activity is unperturbed but Aurora-A recruitment/maintenance at the centrosome is lost, displacing active kinase from centrosomes and causing spindle defects. Drosophila jub genetic mutant analysis, immunofluorescence of Aurora-A localization and activity (phospho-T295), mitotic spindle phenotype quantification Journal of cell science Medium 21402878
2011 Ajuba is required for Rac activation and maintenance of E-cadherin adhesion at cell junctions: Rac activation and actin accumulation at cadherin receptors is impaired in Ajuba-depleted cells. PAK1 directly phosphorylates Ajuba at Thr172; phosphomimetic Ajuba rescues PAK1-inhibition-induced junction defects. Ajuba binds Rac·GDP and Rac·GTP, with phosphorylated Ajuba preferentially interacting with active Rac; Ajuba modulates Rac dynamics at contacts. A Rac-PAK1-Ajuba feedback loop operates at cell-cell contacts. RNAi depletion, in vitro PAK1 kinase assay on Ajuba, phosphomimetic mutant rescue, Rac-GTP pull-down, live imaging of Rac dynamics at junctions The Journal of cell biology High 22105346
2012 Ajuba binds Isl1 transcription factor and represses its transcriptional activity, is required for RA-dependent autorepression of Isl1 expression in the second heart field, and links retinoic acid signaling to Isl1 to restrict cardiac progenitor cell expansion in zebrafish. Co-immunoprecipitation (Ajuba-Isl1), transcriptional reporter assay, Ajuba morpholino knockdown in zebrafish, in situ hybridization of cardiac progenitor markers, RA signaling pathway epistasis Developmental cell Medium 22771034
2013 EGFR-RAS-MAPK signaling promotes phosphorylation of Ajuba family proteins and enhances their binding to Warts/LATS and Salvador/WW45, linking EGFR signaling to Hippo pathway inhibition through Ajuba. In Drosophila, Jub is epistatic to EGFR and Ras for Yorkie regulation. Genetic epistasis in Drosophila (EGFR/Ras/jub double mutants), co-immunoprecipitation (MAPK-promoted binding), MAPK-dependent phosphorylation assay of Ajuba family proteins in mammalian cells Developmental cell High 23484853
2013 JNK promotes phosphorylation of Ajuba family proteins and promotes binding of LIMD1 or WTIP to LATS1, linking JNK to Hippo pathway inhibition; in Drosophila, Jub is required for JNK-mediated Yorkie activation and wing regeneration after wounding. JNK promotes binding of LIMD1 and LATS1 through direct phosphorylation of LIMD1. Genetic epistasis in Drosophila (jub requirement for JNK-Yki axis), biochemical binding assay (co-immunoprecipitation with LATS1), in vitro JNK phosphorylation of LIMD1 Science signaling High 24023255
2013 AJUBA suppresses YAP activity in malignant mesothelioma through LATS2: AJUBA transduction into MM cells suppresses YAP-target gene promoter activities, and this suppression is canceled by LATS2 knockdown, establishing AJUBA as a LATS2-dependent inhibitor of YAP in this cancer context. Lentiviral AJUBA transduction, promoter-reporter assay, siRNA knockdown of LATS2, YAP phosphorylation Western blot Oncogene Medium 24336325
2013 Ajuba associates with the RPA complex and depletion of Ajuba leads to RPA phosphorylation, increased Chk1 phosphorylation, p53 induction, cell cycle delays, and cell death, placing Ajuba as a repressor of unscheduled ATR-mediated DNA damage response. Co-immunoprecipitation with RPA, RNAi depletion, Western blot for Chk1 and RPA phosphorylation, cell cycle analysis Frontiers in genetics Medium 23755068
2014 Increasing cytoskeletal tension promotes Drosophila wing growth via a mechanism involving Ajuba (Jub)-dependent inhibition of Warts kinase: Jub associates with α-catenin at adherens junctions, and this association is promoted by cytoskeletal tension; Jub recruits Warts to junctions in a tension-dependent manner; genetic dependence on Jub links myosin activity to Yorkie regulation. Genetic epistasis (myosin/Jub/Warts double mutants in Drosophila), co-immunoprecipitation of Jub with α-catenin, in vivo imaging of Jub and Warts localization to junctions under tension, wing growth quantification Cell High 24995985
2014 Ajuba activates Aurora-A through two distinct mechanisms: (1) the pre-LIM domain of Ajuba induces autophosphorylation of Aurora-A C-terminal kinase domain and is itself phosphorylated by it; (2) the LIM domain of Ajuba competitively binds to the N-terminal regulatory domain of Aurora-A, disrupting the inhibitory N-terminal/C-terminal intramolecular interaction. In vitro kinase assay with Ajuba domain truncations, co-immunoprecipitation of Ajuba LIM domain with Aurora-A N-terminal domain, competition binding assay Gene Medium 24680704
2015 Ajuba promotes adipogenesis by functioning as an obligate co-activator of PPARγ: Ajuba binds the DNA-binding domain of PPARγ via its preLIM region in a ligand-independent manner, recruits p300/CBP via its LIM domain, and facilitates p300/CBP binding to PPARγ. The Ajuba/PPARγ/p300/CBP complex occupies PPARγ target promoters with increased histone acetylation. Co-immunoprecipitation (Ajuba-PPARγ, Ajuba-p300/CBP), domain mapping by truncation, ChIP at PPARγ target promoters, histone acetylation assay, 3T3-L1 adipogenesis assay with Ajuba KD/OE Cell death and differentiation High 26113042
2016 AJUBA promotes colorectal cancer cell survival by binding the FERM domain of JAK1 to dissociate JAK1 from the IFNγ receptor, inhibiting STAT1 phosphorylation and nuclear translocation, thereby repressing the IFIT2 apoptosis inducer. Co-immunoprecipitation (AJUBA-JAK1 via FERM domain), Western blot for STAT1 phosphorylation, nuclear fractionation, IFIT2 reporter assay, RNAi knockdown Oncogene Medium 27893714
2016 CDK1 phosphorylates Ajuba at Ser119 and Ser175 during G2/M phase of the cell cycle; mitotic phosphorylation of Ajuba promotes cell proliferation and anchorage-independent growth in vitro and tumorigenesis in vivo but does not affect Hippo signaling activity. In vitro CDK1 kinase assay with Ajuba, site-directed mutagenesis (S119A/S175A), cell cycle synchronization, in vivo xenograft tumorigenesis assay The Journal of biological chemistry High 27226586
2016 AJUBA LIM proteins limit Hippo pathway activity in proliferating mammalian epithelial cells by sequestering a cytosolic Hippo kinase complex in which LATS kinase is inhibited; at the plasma membranes of growth-arrested cells, AJUBA LIM proteins do not associate with or inhibit the Hippo kinase complex. AJUBA LIM proteins did not influence YAP activity in response to mechanical signals. Co-immunoprecipitation of AJUBA with LATS in cytosolic fraction, subcellular fractionation, YAP phosphorylation/localization assay in proliferating vs. arrested cells, Drosophila wing growth epistasis Molecular and cellular biology Medium 27457617
2018 The force-sensitive localization of Ajuba to adherens junctions during epithelial morphogenesis requires its N-terminal domain and two of three LIM domains; Ajuba localizes to sites of myosin accumulation within seconds; Ajuba stabilizes adherens junctions in regions of high tension and is required to maintain cell adhesion during cell rearrangement. Live imaging of GFP-Ajuba in Drosophila embryos during axis elongation, domain truncation/mutation analysis of localization, tension perturbation (myosin inhibition/activation), cell-cell adhesion assay The Journal of cell biology Medium 30006462
2018 Ajuba stability in HCC cells is regulated by the E3 ligase Hakai: Hakai interacts with Ajuba via its HYB domain and induces Ajuba neddylation (not ubiquitin-proteasome degradation); neddylation inhibitor MLN4924 but not proteasome inhibitor MG132 antagonizes Hakai-induced Ajuba modification. Co-immunoprecipitation (Hakai-Ajuba via HYB domain), neddylation assay, pharmacological inhibitors (MLN4924, MG132), lentiviral KD/OE Journal of experimental & clinical cancer research : CR Medium 30041665
2018 Ajuba directly interacts with RPA70 subunit of the RPA complex in a cell cycle-regulated manner; the Ajuba-RPA70 interaction is reduced upon DNA replication stress; Ajuba negatively regulates ATR pathway by directly interacting with RPA70 to prevent inappropriate ATR activation. Co-immunoprecipitation, direct protein binding assay (Ajuba-RPA70), cell cycle synchronization, DNA damage stress assay Scientific reports Medium 29934626
2019 Ajuba binds the C-terminus of SP1 transcription factor and functions as a co-activator to enhance SP1 target gene expression; Ajuba is itself a target gene of SP1, forming a feed-forward loop. Ajuba and SP1 co-occupy SP1-responsive promoters as demonstrated by ChIP. Co-immunoprecipitation, GST pull-down, ChIP at SP1 target promoters, luciferase reporter assay Journal of experimental & clinical cancer research : CR Medium 31101117
2019 α-Catenin is the mechanotransducer responsible for tension-dependent recruitment of Jub (Drosophila Ajuba) to adherens junctions: a specific region of α-catenin associates with Jub, and deletion of a region of α-catenin allows constitutive tension-independent Jub recruitment; increased Jub recruitment to α-catenin increases Yorkie activity and wing growth independently of increased cytoskeletal tension. Co-immunoprecipitation (α-catenin-Jub), domain deletion mutants of α-catenin, in vivo Drosophila wing growth assay, Yorkie reporter assay Journal of cell science Medium 30659113
2021 Ajuba is required for PINK1-dependent mitophagy signaling: ZIKV NS5 antagonizes mitophagy by binding Ajuba and preventing its translocation to depolarized mitochondria where it is required for PINK1 activation; mitophagy suppression by NS5-Ajuba binding amplifies pro-inflammatory chemokine production through PKR sensing of mitochondrial RNA. Ajuba-/- mice show enhanced ZIKV dissemination to tissues. Co-immunoprecipitation (ZIKV NS5-Ajuba), live-cell imaging of Ajuba translocation to mitochondria, mitophagy assay, Ajuba knockout mouse ZIKV infection model, PKR signaling assay Cell reports High 34706234
2021 SQSTM1/p62 inhibits Ajuba-induced NF-κB activation in a UBA domain-dependent manner; p62 co-expression reduces nuclear Ajuba localization in unstressed cells; Ajuba is degraded by autophagy but co-expression with p62 (wild type or UBA-deficient) protects Ajuba levels. Co-expression reporter assay for NF-κB, subcellular fractionation, autophagy inhibitor assays, Western blot for Ajuba degradation PloS one Medium 34735553
2021 Ajuba functions as a co-activator of C/EBPβ during adipogenesis: Ajuba interacts with C/EBPβ and recruits CBP to facilitate C/EBPβ binding to promoters of PPARγ and C/EBPα, increasing H3 histone acetylation and target gene expression. Co-immunoprecipitation (Ajuba-C/EBPβ-CBP), ChIP at PPARγ/C/EBPα promoters, histone acetylation assay, 3T3-L1 differentiation assay with Ajuba KD/OE Molecular and cellular endocrinology Medium 34619292
2022 Distinct LIM domains of Drosophila Jub mediate binding to different partners: LIM2 is specifically required for binding to Warts in co-immunoprecipitation and for wing growth/Yorkie regulation in vivo (along with LIM1); LIM2 and LIM3 are required for regulation of cell shape and Steppke binding; multiple regions of Jub contribute to α-catenin binding and junctional localization. LIM domain deletion constructs in Drosophila, co-immunoprecipitation of Jub variants with Warts and Steppke in cultured cells, in vivo wing growth assay, Yorkie activity reporter, cell shape quantification PloS one Medium 35969522
2023 Ajuba is required for slit diaphragm formation and function in nephrocytes: Djub (Drosophila Ajuba homolog) recruits Warts (LATS2 homolog) to the slit diaphragm; Djub knockdown activates the Hippo pathway; Hippo activation reciprocally reduces Djub levels, suggesting a self-amplifying feedback loop. Loss of Djub or Hippo activation causes actin cytoskeleton rearrangement and increased SD permeability. Drosophila nephrocyte genetics, RNAi knockdown, co-immunoprecipitation/localization of Djub and Warts at slit diaphragm, functional permeability assay, in vivo epistasis (Warts KD/Yki overexpression rescue) Journal of the American Society of Nephrology : JASN Medium 36930055
2023 Ajuba is part of a complex with PRMT5 and Aurora-A that shapes the crescent-like Golgi ribbon via modification of HURP: mutual activation of PRMT5 and Aurora-A within the Ajuba/PRMT5/Aurora-A complex leads to arginine methylation then phosphorylation of HURP at p725, which organizes Golgi assembly factors to shape the crescent Golgi ribbon. Co-immunoprecipitation of Ajuba-PRMT5-Aurora-A complex, in vitro kinase/methyltransferase assays, site-directed mutagenesis of HURP phosphorylation site (725A), knockdown-rescue experiment, immunofluorescence of Golgi morphology Cell communication and signaling : CCS Medium 37370099
2023 Ajuba forms a complex with p53 and MDM2 to promote proteasomal degradation of p53; AJUBA overexpression decreases p53 levels without affecting p53 transcription; AJUBA expression is induced by chemotherapeutic drugs in a p53-dependent manner, creating a negative feedback loop. Co-immunoprecipitation (Ajuba-p53-MDM2 complex), Western blot for p53 protein and mRNA (RT-PCR), pharmacological rescue, RNAi knockdown of AJUBA Molecular oncology Medium 36931700
2024 USP7 deubiquitinase interacts with Ajuba and stabilizes it; USP7 knockdown or treatment with USP7 inhibitor FT671 substantially reduces Ajuba protein levels. Both USP7 and Ajuba knockdown reduce cell-cell adhesion in colorectal cancer cells. Co-immunoprecipitation (USP7-Ajuba), quantitative proteomics after inducible USP7 knockdown (LC-MS/MS), pharmacological inhibitor (FT671), cell-cell adhesion assay Molecular & cellular proteomics : MCP Medium 39522755
2025 GSK3β phosphorylates Ajuba at serine 163 within a conserved degron motif (TS163GIS), which mediates interaction with the WD40 domain of β-TrCP E3 ubiquitin ligase (SCFβ-TrCP), leading to ubiquitination and proteasomal degradation of Ajuba. The S163A mutant significantly attenuates Ajuba ubiquitination. In vitro GSK3β kinase assay on Ajuba, co-immunoprecipitation (Ajuba-β-TrCP via WD40 domain), site-directed mutagenesis (S163A), ubiquitination assay Neoplasia (New York, N.Y.) Medium 40367710
2025 Jub (Drosophila Ajuba) promotes phosphorylation of the N-terminal intrinsically disordered region of Warts/LATS, and these N-terminal phosphorylation sites influence Wts recruitment into biomolecular condensates and Wts activity. Jub itself forms condensates that recruit Wts. Minibrain and Homeodomain-interacting protein kinase are identified as kinases promoting Wts N-terminal phosphorylation and modulating condensate recruitment. Condensate formation assay (live imaging of Jub and Wts condensates), phosphorylation assay of Wts N-terminal IDR, mutagenesis of N-terminal phosphorylation sites, genetic epistasis in Drosophila, kinase identification by genetics Cell reports Medium 41351836
2017 Ajuba interacts with Twist transcription factor via its LIM domain (Twist box is required); Ajuba functions as an obligate co-activator of Twist to enhance N-cadherin transcription; Ajuba recruits CBP and Twist to form a ternary complex at the N-cadherin promoter E-box with concomitant histone acetylation. Co-immunoprecipitation (Ajuba-Twist), domain mutagenesis, luciferase reporter assay, ChIP at N-cadherin promoter, histone acetylation assay Journal of cellular and molecular medicine Medium 34173718
2025 APC loss stabilizes Ajuba protein through GSK-3 dysregulation (independent of β-catenin); stabilized Ajuba acts as a positive regulator of YAP, driving a fetal intestinal transcriptional program that is mutually exclusive with β-catenin-driven transcription, contributing to bistable tumor-initiating states. APC knockout intestinal organoids vs. β-CATENIN activation mutants, Ajuba protein stability assay under GSK-3 inhibition, YAP transcriptional reporter, epistasis (APC-Ajuba-YAP pathway), single-cell transcriptomics bioRxivpreprint Low bio_10.1101_2025.03.06.641686
2010 In medaka, Ajuba localizes to basal bodies of cilia in growth-arrested cells and is essential for ciliogenesis in Kupffer's vesicle cells; Ajuba knockdown results in randomized left-right organ asymmetry and altered expression of left-right body axis determination genes, establishing a role in vertebrate ciliogenesis. Medaka Ajuba knockdown (morpholino), immunofluorescence of Ajuba at basal bodies, ciliogenesis assay in Kupffer's vesicle cells, in situ hybridization of laterality markers Biochemical and biophysical research communications Medium 20457130
2017 Ajuba suppresses CdGAP (a Rac1/Cdc42 GAP) activity at epithelial cell-cell contacts: Ajuba interacts with CdGAP via distinct domains from those used for Rac1 binding; Ajuba binding inhibits CdGAP GAP activity; CdGAP recruitment to junctions does not require Ajuba, but Ajuba controls CdGAP residence at contacts. Co-immunoprecipitation (Ajuba-CdGAP), in vitro GAP activity assay, immunofluorescence of CdGAP/Ajuba localization, domain mapping Scientific reports Medium 28835688
2022 Over-expression of AJUBA or WTIP in MCF10A cells displaces LIMD1 from adherens junctions (competitive binding) and reduces LATS1 junctional localization, associated with increased YAP1 phosphorylation and decreased nuclear YAP1, suggesting AJUBA and WTIP have activities distinct from LIMD1 in Hippo regulation at junctions. Overexpression of AJUBA/WTIP, immunofluorescence of LIMD1 and LATS1 junctional localization, YAP1 phosphorylation and nuclear localization Western blot/imaging microPublication biology Low 36439396

Source papers

Stage 0 corpus · 87 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2003 Aurora-A and an interacting activator, the LIM protein Ajuba, are required for mitotic commitment in human cells. Cell 545 13678582
2014 Cytoskeletal tension inhibits Hippo signaling through an Ajuba-Warts complex. Cell 277 24995985
2013 Regulation of Hippo signaling by EGFR-MAPK signaling through Ajuba family proteins. Developmental cell 235 23484853
2010 Ajuba LIM proteins are negative regulators of the Hippo signaling pathway. Current biology : CB 212 20303269
2008 The LIM protein AJUBA recruits protein arginine methyltransferase 5 to mediate SNAIL-dependent transcriptional repression. Molecular and cellular biology 181 18347060
2013 Ajuba family proteins link JNK to Hippo signaling. Science signaling 129 24023255
2002 The LIM protein Ajuba is recruited to cadherin-dependent cell junctions through an association with alpha-catenin. The Journal of biological chemistry 127 12417594
2000 Ajuba, a cytosolic LIM protein, shuttles into the nucleus and affects embryonal cell proliferation and fate decisions. Molecular biology of the cell 116 11029037
2005 The LIM protein Ajuba influences p130Cas localization and Rac1 activity during cell migration. The Journal of cell biology 97 15728191
1999 Ajuba, a novel LIM protein, interacts with Grb2, augments mitogen-activated protein kinase activity in fibroblasts, and promotes meiotic maturation of Xenopus oocytes in a Grb2- and Ras-dependent manner. Molecular and cellular biology 93 10330178
2006 LATS2-Ajuba complex regulates gamma-tubulin recruitment to centrosomes and spindle organization during mitosis. FEBS letters 82 16413547
2005 The LIM protein Ajuba influences interleukin-1-induced NF-kappaB activation by affecting the assembly and activity of the protein kinase Czeta/p62/TRAF6 signaling complex. Molecular and cellular biology 72 15870274
2011 Ajuba is required for Rac activation and maintenance of E-cadherin adhesion. The Journal of cell biology 68 22105346
2012 The LIM protein Ajuba restricts the second heart field progenitor pool by regulating Isl1 activity. Developmental cell 67 22771034
2013 LIM-domain protein AJUBA suppresses malignant mesothelioma cell proliferation via Hippo signaling cascade. Oncogene 66 24336325
2016 The LIM protein AJUBA promotes colorectal cancer cell survival through suppression of JAK1/STAT1/IFIT2 network. Oncogene 61 27893714
2007 The Ajuba LIM domain protein is a corepressor for SNAG domain mediated repression and participates in nucleocytoplasmic Shuttling. Cancer research 57 17909014
2005 The LIM protein Ajuba regulates phosphatidylinositol 4,5-bisphosphate levels in migrating cells through an interaction with and activation of PIPKI alpha. Molecular and cellular biology 57 15870270
2010 LIM-domain proteins, LIMD1, Ajuba, and WTIP are required for microRNA-mediated gene silencing. Proceedings of the National Academy of Sciences of the United States of America 53 20616046
2007 Ajuba negatively regulates the Wnt signaling pathway by promoting GSK-3beta-mediated phosphorylation of beta-catenin. Oncogene 53 17621269
2018 The force-sensitive protein Ajuba regulates cell adhesion during epithelial morphogenesis. The Journal of cell biology 52 30006462
2008 Ajuba functions as a histone deacetylase-dependent co-repressor for autoregulation of the growth factor-independent-1 transcription factor. The Journal of biological chemistry 52 18805794
2016 AJUBA LIM Proteins Limit Hippo Activity in Proliferating Cells by Sequestering the Hippo Core Kinase Complex in the Cytosol. Molecular and cellular biology 51 27457617
2020 Hsa_circ_0128846 promotes tumorigenesis of colorectal cancer by sponging hsa-miR-1184 and releasing AJUBA and inactivating Hippo/YAP signalling. Journal of cellular and molecular medicine 48 32681581
2018 Ajuba inhibits hepatocellular carcinoma cell growth via targeting of β-catenin and YAP signaling and is regulated by E3 ligase Hakai through neddylation. Journal of experimental & clinical cancer research : CR 45 30041665
2017 AJUBA increases the cisplatin resistance through hippo pathway in cervical cancer. Gene 45 29126926
2010 LIM protein Ajuba functions as a nuclear receptor corepressor and negatively regulates retinoic acid signaling. Proceedings of the National Academy of Sciences of the United States of America 44 20133701
2016 Ajuba Phosphorylation by CDK1 Promotes Cell Proliferation and Tumorigenesis. The Journal of biological chemistry 43 27226586
2021 Mitophagy antagonism by ZIKV reveals Ajuba as a regulator of PINK1 signaling, PKR-dependent inflammation, and viral invasion of tissues. Cell reports 41 34706234
2020 Super-enhancer-driven AJUBA is activated by TCF4 and involved in epithelial-mesenchymal transition in the progression of Hepatocellular Carcinoma. Theranostics 39 32802179
2011 Drosophila Ajuba is not an Aurora-A activator but is required to maintain Aurora-A at the centrosome. Journal of cell science 38 21402878
2019 Ajuba overexpression regulates mitochondrial potential and glucose uptake through YAP/Bcl-xL/GLUT1 in human gastric cancer. Gene 35 30690182
2016 AJUBA promotes the migration and invasion of esophageal squamous cell carcinoma cells through upregulation of MMP10 and MMP13 expression. Oncotarget 35 27172796
2019 Recruitment of Jub by α-catenin promotes Yki activity and Drosophila wing growth. Journal of cell science 34 30659113
2002 The amino terminus of the glial glutamate transporter GLT-1 interacts with the LIM protein Ajuba. Molecular and cellular neurosciences 34 11860269
2017 Androgen receptor-regulated miRNA-193a-3p targets AJUBA to promote prostate cancer cell migration. The Prostate 31 28422308
2015 The LIM protein Ajuba promotes adipogenesis by enhancing PPARγ and p300/CBP interaction. Cell death and differentiation 31 26113042
2019 The LIM protein Ajuba/SP1 complex forms a feed forward loop to induce SP1 target genes and promote pancreatic cancer cell proliferation. Journal of experimental & clinical cancer research : CR 27 31101117
2019 Ajuba: An emerging signal transducer in oncogenesis. Pharmacological research 27 31740385
2014 LIM protein JUB promotes epithelial-mesenchymal transition in colorectal cancer. Cancer science 26 24673742
2017 Mutations of the LIM protein AJUBA mediate sensitivity of head and neck squamous cell carcinoma to treatment with cell-cycle inhibitors. Cancer letters 24 28126323
2017 Smad1 promotes colorectal cancer cell migration through Ajuba transactivation. Oncotarget 23 29299158
2021 AJUBA: A regulator of epidermal homeostasis and cancer. Experimental dermatology 21 33372298
2009 Ajuba: a new microtubule-associated protein that interacts with BUBR1 and Aurora B at kinetochores in metaphase. Biology of the cell 21 18710370
2018 The Ajuba family protein Wtip regulates actomyosin contractility during vertebrate neural tube closure. Journal of cell science 18 29661847
2023 Activation of Hippo Pathway Damages Slit Diaphragm by Deprivation of Ajuba Proteins. Journal of the American Society of Nephrology : JASN 17 36930055
2018 Ajuba receptor mediates the internalization of tumor-secreted GRP78 into macrophages through different endocytosis pathways. Oncotarget 17 29643986
2021 Ajuba functions as a co-activator of C/EBPβ to induce expression of PPARγ and C/EBPα during adipogenesis. Molecular and cellular endocrinology 16 34619292
2021 The SQSTM1/p62 UBA domain regulates Ajuba localisation, degradation and NF-κB signalling function. PloS one 16 34735553
2014 A novel mechanism for activation of Aurora-A kinase by Ajuba. Gene 16 24680704
2013 LIM Protein Ajuba Participates in the Repression of the ATR-Mediated DNA Damage Response. Frontiers in genetics 16 23755068
2020 The LIM Protein Ajuba Augments Tumor Metastasis in Colon Cancer. Cancers 13 32679899
2022 Ajuba Overexpression Promotes Breast Cancer Chemoresistance and Glucose Uptake through TAZ-GLUT3/Survivin Pathway. BioMed research international 12 35178446
2017 The scaffold protein Ajuba suppresses CdGAP activity in epithelia to maintain stable cell-cell contacts. Scientific reports 11 28835688
2010 The LIM protein Ajuba is required for ciliogenesis and left-right axis determination in medaka. Biochemical and biophysical research communications 11 20457130
2021 Ajuba transactivates N-cadherin expression in colorectal cancer cells through interaction with Twist. Journal of cellular and molecular medicine 10 34173718
2018 Clinical significance of AJUBA, YAP1, and MMP14 expression in esophageal squamous cell carcinoma. International journal of clinical and experimental pathology 10 31949690
2021 miR-433-3p Targets AJUBA to Inhibit Malignant Progression of Glioma. Neuroimmunomodulation 9 34518486
2022 Analysis of the Drosophila Ajuba LIM protein defines functions for distinct LIM domains. PloS one 7 35969522
2018 LIM Protein Ajuba associates with the RPA complex through direct cell cycle-dependent interaction with the RPA70 subunit. Scientific reports 6 29934626
2014 Aurora-A kinase-inactive mutants disrupt the interaction with Ajuba and cause defects in mitotic spindle formation and G2/M phase arrest in HeLa cells. BMB reports 6 24499673
2024 Transcription factor EHF interacting with coactivator AJUBA aggravates malignancy and acts as a therapeutic target for gastroesophageal adenocarcinoma. Acta pharmaceutica Sinica. B 5 38799645
2022 MiRNA-21 promotes differentiation of bone marrow mesenchymal stem cells into cardiomyocyte-like cells by regulating the Ajuba/Isl1 axis pathway. Archives of medical science : AMS 5 36457985
2022 LIM protein Ajuba promotes liver cell proliferation through its involvement in DNA replication and DNA damage control. FEBS letters 4 35535434
2021 Knockout of Ajuba Attenuates the Growth and Migration of Hepatocellular Carcinoma Cells. Cytogenetic and genome research 4 33640888
2021 Evidence for AJUBA-catenin-CDH4-linked differentiation resistance of mesenchymal stem cells implies tumorigenesis and progression of head and neck squamous cell carcinoma: a single-cell transcriptome approach. Blood and genomics 4 34368804
2025 AJUBA promotes the proliferation, invasion and migration of NSCLC cells by activating the ERK/β-catenin pathway. Scientific reports 3 40240814
2023 The crescent-like Golgi ribbon is shaped by the Ajuba/PRMT5/Aurora-A complex-modified HURP. Cell communication and signaling : CCS 3 37370099
2023 Multitarget Protective Effects of JUB on Aβ-Induced Neurotoxicity and the Mechanism Predication Using Network Pharmacology Analysis. Journal of agricultural and food chemistry 3 38098161
2022 AJUBA and WTIP can compete with LIMD1 for junctional localization and LATS regulation. microPublication biology 3 36439396
2023 LIM domain-containing protein Ajuba inhibits chemotherapy-induced apoptosis by negatively regulating p53 stability in colorectal cancer cells. Molecular oncology 2 36931700
2023 Case Report: Identification of a novel NTRK3-AJUBA fusion co-existing with ETV6-NTRK3 fusion in papillary thyroid carcinoma. Frontiers in oncology 2 37188179
2014 Molecular cloning and expression analysis of the Ajuba gene of grass carp (Ctenopharyngodon idella) involved in cellular response to viral infection. Developmental and comparative immunology 2 25452047
2025 Exosome- transported FER inhibitor suppresses progression of diffuse large B-cell lymphoma via regulating AJUBA/Hippo axis. NPJ precision oncology 1 40707658
2025 External stent ameliorates vein graft remodeling through Ajuba-mediated suppression of Hippo signaling pathway. Biomaterials advances 1 40743849
2025 Jub-induced phosphorylation of Warts inhibits its activity and recruitment into biomolecular condensates. Cell reports 1 41351836
2025 Phase-Separation of YAP Mediates AJUBA Super Enhancer Activation to Promote Aberrant Mitosis in Breast Cancer. Advanced science (Weinheim, Baden-Wurttemberg, Germany) 1 41355615
2023 Peripodial adherens junctions regulate Ajuba-Yorkie signaling to preserve fly eye morphology. Biology open 1 36912729
2018 JUB induces epithelial-mesenchymal transition via the Wnt/β-catenin signaling pathway in hepatocellular carcinoma cells. International journal of clinical and experimental pathology 1 31938233
2026 AJUBA Attenuates Pathological Cardiac Hypertrophy by Enhancing NEDD4-Mediated Ubiquitination and Degradation of DVL2. Cell biology international 0 41793265
2026 AJUBA: The Master Regulator Bridging EMT and Immune Evasion in Colorectal Cancer. Mediators of inflammation 0 41814682
2025 SCFβ-TrCP targets Ajuba for degradation in a GSK3β-dependent manner in colorectal cancer. Neoplasia (New York, N.Y.) 0 40367710
2025 Ajuba as a Potential Nutrition-Responsive Biomarker for the Prevention of Age-Related Sarcopenia. International journal of molecular sciences 0 40869189
2024 Knockdown Proteomics Reveals USP7 as a Regulator of Cell-Cell Adhesion in Colorectal Cancer via AJUBA. Molecular & cellular proteomics : MCP 0 39522755
2024 Targeting the Ajuba/Notch axis increases the sensitivity of colon cancer cells to 5-fluorouracil. CytoJournal 0 39737130
2022 Evaluation of Immunoexpression of AJUBA Protein in Normal Oral Mucosa and Oral Squamous Cell Carcinoma. Applied immunohistochemistry & molecular morphology : AIMM 0 36222508
2015 siRNA-mediated knockdown of JUB expression suppresses the proliferation of glioblastoma cells. Cancer biomarkers : section A of Disease markers 0 26406867

Missed literature

Know a paper Affinage missed for AJUBA? Flag it for the maintainers and the community.

No submissions yet.