Affinage

CBY1

Protein chibby homolog 1 · UniProt Q9Y3M2

Length
126 aa
Mass
14.5 kDa
Annotated
2026-04-28
66 papers in source corpus 27 papers cited in narrative 27 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

CBY1 (Chibby1) is a conserved, partially disordered coiled-coil protein that functions both as an antagonist of canonical Wnt/β-catenin signaling and as an essential regulator of ciliogenesis. CBY1 directly binds the C-terminal activation domain of β-catenin, competing with Tcf/Lef transcription factors to repress β-catenin-mediated transcription; Akt phosphorylation of CBY1 at Ser20 creates a 14-3-3 binding motif, enabling formation of a tripartite CBY1–14-3-3–β-catenin complex that is exported from the nucleus via CRM1-dependent transport (PMID:12712206, PMID:18573912, PMID:19940019). At centrioles, CBY1 localizes to a distal appendage ring on the mother centriole (recruited by CEP164 and Cenexin/ODF2), where it promotes ciliary vesicle formation through Rabin8/Rab8 recruitment, facilitates Ahi1 transition zone assembly, and cooperates with the BAR-domain proteins FAM92A/B to remodel membranes during basal body docking (PMID:25313408, PMID:25103236, PMID:27528616, PMID:40484380). Biallelic loss-of-function variants in CBY1 cause Joubert syndrome in humans, and Cby1-knockout mice exhibit primary ciliary dyskinesia-like airway defects, cystic kidneys, and exocrine pancreatic degeneration (PMID:33131181, PMID:19364920, PMID:34446743).

Mechanistic history

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

    The fundamental question of CBY1's molecular function was answered: it directly binds the C-terminus of β-catenin and competitively inhibits Tcf/Lef-dependent transcription, establishing CBY1 as a nuclear antagonist of canonical Wnt signaling.

    Evidence Protein interaction screen, competition binding assay, and Drosophila genetic epistasis (Nature)

    PMID:12712206

    Open questions at the time
    • Mechanism of CBY1 recruitment to β-catenin unknown
    • No structural detail of the CBY1–β-catenin interface
    • Whether CBY1 functions outside Wnt signaling was unexplored
  2. 2004 Medium

    An independent screen revealed that CBY1 interacts with polycystin-2 and may regulate its intracellular trafficking to the trans-Golgi network, providing the first hint of a cilia/polycystin-related role for CBY1.

    Evidence Yeast two-hybrid screen and co-expression/immunofluorescence in LLC-PK1 and HeLa cells

    PMID:15194699

    Open questions at the time
    • Functional consequence of CBY1–PC2 interaction on ciliary signaling not tested
    • No in vivo validation
    • No reciprocal pulldown from endogenous PC2
  3. 2006 Medium

    TC-1 (C8orf4) was identified as a binding partner that antagonizes CBY1's repression of β-catenin, establishing that CBY1's Wnt-inhibitory activity is itself subject to regulation by competing interactors.

    Evidence Co-immunoprecipitation and TOPflash reporter assay in cancer cells

    PMID:16424001

    Open questions at the time
    • No mutagenesis mapping of the TC-1–CBY1 interface at the time
    • Physiological context of TC-1 regulation of CBY1 unclear
  4. 2007 High

    CBY1's role in adipocyte differentiation demonstrated that its β-catenin antagonism has developmental consequences: CBY1 promotes adipogenesis by relieving Wnt/β-catenin-mediated suppression of differentiation.

    Evidence Gain- and loss-of-function in 3T3-L1 cells and Cby-deficient MEFs

    PMID:17403895

    Open questions at the time
    • Whether CBY1 regulates adipogenesis through β-catenin-independent mechanisms not addressed
    • In vivo adipose phenotype in KO mice not characterized
  5. 2008 High

    The mechanism by which CBY1 clears β-catenin from the nucleus was resolved: Akt phosphorylation at Ser20 creates a 14-3-3 binding site, and the resulting tripartite CBY1–14-3-3–β-catenin complex partitions β-catenin to the cytoplasm.

    Evidence AP-MS, site-directed mutagenesis of S20, co-IP, subcellular fractionation (J. Cell Biol.)

    PMID:18573912

    Open questions at the time
    • Structural basis of 14-3-3 recognition of phospho-CBY1 not yet determined
    • Nuclear export route not characterized
  6. 2009 High

    Three key structural and functional properties were established simultaneously: CBY1 contains functional NLS/NES motifs and shuttles between nucleus and cytoplasm via CRM1; CBY1 homodimerizes through a C-terminal coiled-coil required for nuclear import; and Cby-knockout mice lack motile cilia due to failed basal body docking, revealing CBY1's essential role in ciliogenesis.

    Evidence NLS/NES mutagenesis with leptomycin B and live imaging; coiled-coil alanine scanning and SEC; Cby−/− mouse with EM and mucociliary transport assays

    PMID:19364920 PMID:19435523 PMID:19940019

    Open questions at the time
    • How CBY1's Wnt and cilia functions are coordinated at the same protein was unclear
    • Mechanism of basal body docking failure not resolved at the molecular level
  7. 2010 High

    CBY1 was placed downstream of the master ciliogenesis transcription factor Foxj1 and shown to be essential for lung epithelial development, linking its transcriptional regulation to its basal body/cilia function in vivo.

    Evidence Cby−/− mouse lung analysis, Foxj1 promoter analysis, immunofluorescence, EM

    PMID:21049041

    Open questions at the time
    • Whether Foxj1 is the sole transcriptional regulator of Cby1 not determined
    • Alveolar enlargement phenotype mechanism not molecularly defined
  8. 2011 High

    The biophysical architecture of CBY1 was resolved: its N-terminal half is intrinsically disordered (harboring the 14-3-3 binding region), while its C-terminal coiled-coil mediates homodimerization and TC-1 binding, establishing a modular structure-function framework.

    Evidence NMR spectroscopy, ESI-MS, CD, and DLS on full-length CBY1

    PMID:21182262

    Open questions at the time
    • Full-length CBY1 structure in complex with β-catenin not determined
    • How disorder-to-order transitions regulate partner selectivity unknown
  9. 2012 High

    CBY1's centriolar location was pinpointed to the distal end of the mother centriole, dependent on Cenexin/ODF2 recruitment, and Drosophila Cby was shown to localize to the basal body transition zone and be required for ciliary structure but dispensable for Wingless signaling—clarifying that the cilia function is the conserved ancestral role.

    Evidence Mammalian co-IP and siRNA with immunofluorescence; Drosophila cby mutant with EM and sensory assays

    PMID:22508513 PMID:22911743

    Open questions at the time
    • The precise distal appendage substructure where CBY1 sits was not yet resolved at nanometer resolution
    • Why Drosophila Cby is dispensable for Wnt but mammalian CBY1 is not was unresolved
  10. 2014 High

    The molecular pathway by which CBY1 promotes ciliogenesis was elaborated: CBY1 is recruited to distal appendages by CEP164, then engages Rabin8 to activate Rab8 and form ciliary vesicles; superresolution microscopy resolved CBY1 to an ~250-nm ring, and its loss impairs Ahi1 transition zone assembly and causes cystic kidneys.

    Evidence Co-IP of CBY1–CEP164 and CBY1–Rabin8 in primary MTECs; 3D-SIM/STED in Cby1-KO cells; KO mouse kidney phenotype

    PMID:25103236 PMID:25313408

    Open questions at the time
    • Whether CBY1 directly activates Rabin8 or serves as a scaffold unknown
    • Structural basis of the CBY1–CEP164 interaction not determined
  11. 2015 High

    The atomic basis of 14-3-3 recognition was established (2.2 Å crystal structure of 14-3-3ζ–phospho-CBY1 peptide), and separately, CBY1 was shown to be required for proper IFT-B distribution in cilia—its loss causes paddle-like cilia with IFT-B accumulation at tips.

    Evidence X-ray crystallography, NMR, and ITC for 14-3-3 structure; Cby−/− mouse MTECs and MEFs with IFT subcomplex immunofluorescence

    PMID:25909186 PMID:26266958

    Open questions at the time
    • How CBY1 specifically affects IFT-B but not IFT-A turnover is mechanistically unexplained
    • Whether IFT defects are secondary to basal body docking failure was not fully resolved
  12. 2016 High

    FAM92A and FAM92B were identified as CBY1 interactors that depend on CBY1 for centriolar localization and cooperate with it in Rab8-dependent membrane remodeling, establishing the CBY1–FAM92 module as a membrane-shaping unit at basal bodies.

    Evidence Tandem affinity purification/MS, co-IP, siRNA, and ciliogenesis assays

    PMID:27528616

    Open questions at the time
    • Structural basis of FAM92–CBY1 interaction unknown at the time
    • Whether FAM92 BAR domain directly tubulates membranes in a CBY1-dependent manner was not shown
  13. 2020 High

    The clinical significance of CBY1 was established: biallelic loss-of-function variants cause Joubert syndrome in humans, with patient fibroblasts showing reduced ciliation, elongated cilia, and reduced AHI1/ARL13B—directly linking the mouse cilia phenotype to a human ciliopathy.

    Evidence Human genetic analysis (biallelic LOF), patient fibroblast immunofluorescence, zebrafish morpholino knockdown

    PMID:33131181

    Open questions at the time
    • Genotype-phenotype correlations across different CBY1 mutations not yet characterized
    • Whether CBY1 loss-of-function contributes to a broader spectrum of ciliopathies unknown
  14. 2021 High

    CBY1's role was extended to two additional tissues: DZIP1 forms a complex with CBY1 and β-catenin at cardiac valve basal bodies to suppress β-catenin and prevent myxomatous degeneration, and Cby1-KO mice develop severe exocrine pancreatic atrophy with defective zymogen secretion, broadening the phenotypic spectrum.

    Evidence Co-IP and decoy peptide experiments in cardiac valves; Cby1-KO mouse pancreas EM and ex vivo secretion assays

    PMID:33811421 PMID:34446743

    Open questions at the time
    • Whether pancreatic defects are purely cilia-dependent or involve CBY1's Wnt function not resolved
    • DZIP1–CBY1 complex stoichiometry and structure unknown
  15. 2024 Medium

    Genetic epistasis in Drosophila established that the Cby–Fam92 module and the Cep131–Cep162 module cooperatively maintain Cep290 at the basal body, and concurrent loss blocks ciliogenesis initiation, placing CBY1 in a defined pathway hierarchy for transition zone assembly.

    Evidence Drosophila double mutants with immunofluorescence and epistasis analysis

    PMID:38442096

    Open questions at the time
    • Whether this pathway hierarchy is conserved in mammals not yet tested
    • Direct physical interaction between Cby–Fam92 module and Cep290 not demonstrated
  16. 2025 High

    The structural basis of the CBY1–FAM92A interaction was resolved: a 2.2 Å crystal structure of the FAM92A BAR domain revealed an antiparallel crescent homodimer, and FAM92A binds the N-terminal region of CBY1, with dimerization of both proteins synergistically enhancing affinity.

    Evidence X-ray crystallography, structure-guided mutagenesis, co-IP, binding affinity measurements

    PMID:40484380

    Open questions at the time
    • Structure of a full CBY1–FAM92A complex on membranes not determined
    • How FAM92A lipid binding coordinates with CBY1-mediated Rab8 recruitment is undefined

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include: how CBY1's dual Wnt-inhibitory and ciliogenic functions are spatiotemporally coordinated within the same cell; the atomic structure of the CBY1–β-catenin complex; and the full genotype-phenotype spectrum of human CBY1 ciliopathies.
  • No structure of full-length CBY1 in complex with β-catenin
  • Mechanism by which CBY1 selectively affects IFT-B versus IFT-A not molecularly explained
  • How Foxj1-driven transcription of Cby1 is integrated with post-translational regulation (Akt, 14-3-3) is unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 3 GO:0098772 molecular function regulator activity 3
Localization
GO:0005815 microtubule organizing center 4 GO:0005634 nucleus 3 GO:0005929 cilium 3 GO:0005829 cytosol 2
Pathway
R-HSA-162582 Signal Transduction 4 R-HSA-1852241 Organelle biogenesis and maintenance 4 R-HSA-1266738 Developmental Biology 3
Partners
CEP164CTNNB1FAM92AFAM92BODF2RABIN8YWHAEYWHAZ
Complex memberships
CBY1–14-3-3–β-catenin tripartite complexCBY1–FAM92A/B membrane-remodeling moduleDZIP1–CBY1–β-catenin basal body complex

Evidence

Reading pass · 27 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2003 CBY1 (Chibby) was identified as a nuclear protein that directly interacts with the C-terminal region of β-catenin and inhibits β-catenin-mediated transcriptional activation by competing with Lef-1 for binding to β-catenin. Epistasis experiments in Drosophila placed chibby downstream of wingless and upstream of armadillo. Protein interaction screen, competition binding assay, RNAi in Drosophila, genetic epistasis Nature High 12712206
2008 CBY1 cooperates with 14-3-3ε and 14-3-3ζ to facilitate nuclear export of β-catenin. Akt kinase phosphorylates CBY1 at serine 20, which creates a 14-3-3 binding motif; 14-3-3 binding sequesters CBY1 in the cytoplasm and CBY1, 14-3-3, and β-catenin form a stable tripartite complex causing β-catenin to partition into the cytoplasm. Affinity purification/mass spectrometry, site-directed mutagenesis (S20), co-immunoprecipitation, subcellular fractionation The Journal of cell biology High 18573912
2009 CBY1 harbors bona fide nuclear localization signal (NLS) and nuclear export signal (NES) motifs and constitutively shuttles between nucleus and cytoplasm. Efficient nuclear export requires cooperative action of the intrinsic NES, 14-3-3, and CRM1 nuclear export receptor. 14-3-3 docking promotes CBY1 binding to CRM1 while inhibiting its interaction with importin-α, and NLS/NES-dependent shuttling of CBY1 modulates β-catenin intracellular localization. NLS/NES mutagenesis, nuclear export inhibitor (leptomycin B), shRNA knockdown, co-immunoprecipitation, live cell imaging Molecular biology of the cell High 19940019
2009 CBY1 forms a stable homodimer through a heptad repeat of four leucine residues in its C-terminal coiled-coil motif. Alanine substitution of two or more leucine residues abolishes homodimerization. Homodimerization is required for efficient interaction with importin-α and subsequent nuclear translocation, but monomeric CBY1 retains the ability to bind β-catenin and repress its transcriptional activity. Alanine scanning mutagenesis, co-immunoprecipitation, size exclusion chromatography BMC molecular biology High 19435523
2009 CBY1 is localized at the base of cilia in mouse nasal epithelium, and Cby−/− mice exhibit impaired basal body docking to the apical surface of multiciliated cells, resulting in a marked paucity of motile cilia and complete absence of mucociliary transport. Cby knockout mouse, immunofluorescence localization, electron microscopy of basal body docking, mucociliary transport assay The Journal of cell biology High 19364920
2007 CBY1 promotes adipocyte differentiation by inhibiting β-catenin signaling. Ectopic expression of CBY1 induces spontaneous differentiation of 3T3-L1 preadipocytes, while RNAi depletion of CBY1 blocks adipogenesis. Embryonic fibroblasts from Cby-deficient embryos show attenuated adipogenic differentiation. RNAi knockdown, ectopic overexpression, Cby-deficient mouse embryonic fibroblasts, adipogenic differentiation assay Molecular and cellular biology High 17403895
2012 CBY1 is a centriolar component specifically located at the distal end of the mother centriole and is essential for assembly of the primary cilium. CBY1 interacts physically with the distal appendage component Cenexin (ODF2), which abrogates CBY1's inhibitory effect on β-catenin-mediated transcription in a dose-dependent manner. Cenexin is required for recruitment of CBY1 to the mother centriole, but CBY1 is dispensable for Cenexin localization. Co-immunoprecipitation, immunofluorescence localization, siRNA knockdown, TOPflash reporter assay PloS one High 22911743
2012 In Drosophila, CBY localizes to the basal body transition zone in sensory neurons and male germ cells, and is required for basal body structure and ciliary function, including proper ciliary protein trafficking and axonemal assembly, but is not required for Wingless signaling in flies. cby mutant Drosophila, immunofluorescence, electron microscopy, sensory transduction assays The Journal of cell biology High 22508513
2014 CBY1 facilitates basal body docking to the apical cell membrane during airway multiciliated cell differentiation through proper formation of ciliary vesicles at distal appendages. CBY1 is recruited to distal appendages via physical interaction with CEP164, then associates with Rabin8 (a GEF for Rab8) to promote Rab8 recruitment and efficient assembly of ciliary vesicles. Primary mouse tracheal epithelial cell cultures, co-immunoprecipitation, RNAi knockdown, immunofluorescence, electron microscopy The Journal of cell biology High 25313408
2014 CBY1 localizes to an ~250-nm ring at the distal end of the mature centriole (dependent on ODF1/Ofd1) and promotes the recruitment of Ahi1 to the transition zone. In Cby1-knockout cells, centriole-localized Ahi1 is reduced, impairing ciliogenesis and ciliary recruitment of the Joubert syndrome protein Arl13b. CBY1 deletion causes cystic kidneys in mice. 3D-SIM and STED superresolution microscopy, Cby1 knockout mouse, immunofluorescence, quantitative localization analysis Molecular biology of the cell High 25103236
2015 The crystal structure of the human 14-3-3ζ/CBY1 peptide complex was solved at 2.2 Å, revealing a canonical binding mode where phosphorylation of S20 is essential for 14-3-3 recognition. NMR titration shows that residues outside the conserved 14-3-3 binding cleft (flexible loop residues 203-210) also contribute to the interaction. X-ray crystallography, NMR spectroscopy, isothermal titration calorimetry, mutagenesis PloS one High 25909186
2015 CBY1 is required for normal ciliary morphology and proper distribution of IFT-B complex proteins (IFT88, IFT20, IFT57) but not IFT-A or BBS proteins in airway ciliated cells. Loss of CBY1 causes paddle-like cilia with dilated tips and accumulation of IFT-B components within those tips. Cby knockout mouse, primary MTECs, Cby-/- MEFs, immunofluorescence, electron microscopy Cell cycle High 26266958
2016 FAM92A and FAM92B (BAR domain-containing proteins) interact with CBY1 and colocalize with it at centrioles/basal bodies. Centriolar localization of FAM92A and FAM92B depends largely on CBY1. FAM92A knockdown impairs ciliogenesis. FAM92A and FAM92B, in cooperation with CBY1, induce Rab8-containing membrane-remodeling structures. Tandem affinity purification/mass spectrometry, co-immunoprecipitation, siRNA knockdown, immunofluorescence, ciliogenesis assay Molecular and cellular biology High 27528616
2006 TC1 (C8orf4) interacts with CBY1 and antagonizes CBY1's inhibitory function on β-catenin-mediated transcription, thereby acting as a positive regulator of the Wnt/β-catenin pathway. Co-expression of TC1 and CBY1 results in relocalization of TC1 from nucleolus to nuclear speckles where it colocalizes with CBY1. Co-immunoprecipitation, TOPflash reporter assay, immunofluorescence colocalization Cancer research Medium 16424001
2007 TC-1 (thyroid cancer-1), an intrinsically disordered protein, interacts with CBY1 via three regions with high helical propensity (D44-R53, K58-A64, D73-T88) in its C-terminal portion, as determined by NMR spectroscopy. NMR spectroscopy (chemical shift analysis, relaxation measurements, resonance broadening) Protein science High 17905836
2011 Human CBY1 is a partially disordered protein: its N-terminal portion is predominantly unstructured in solution while the C-terminal half adopts a coiled-coil structure through self-association. CBY1 uses its N-terminal disordered module to bind 14-3-3ζ and its C-terminal coiled-coil for self-association and TC-1 binding. NMR spectroscopy, ESI-MS, CD, DLS Biochemistry High 21182262
2004 CBY1 (PIGEA-14) was identified as an interacting partner of the C-terminus of polycystin-2 (PC2) via yeast two-hybrid screen. Co-expression of CBY1 and PC2 in LLC-PK1 and HeLa cells caused redistribution of both proteins to the trans-Golgi network, suggesting CBY1 regulates intracellular trafficking of PC2. CBY1 also interacts with GM130, a cis-Golgi component. Yeast two-hybrid screen, co-expression/immunofluorescence localization, co-immunoprecipitation The Journal of biological chemistry Medium 15194699
2010 CBY1 protein is prominently associated with centrosome/basal body microtubule structures in embryonic lung epithelial progenitor cells and at the base of motile cilia in airway ciliated cells. CBY1 is a direct downstream transcriptional target of the master ciliogenesis transcription factor Foxj1. Loss of CBY1 results in alveolar airspace enlargement with reduced proliferation, abnormal epithelial cell differentiation, and failure of basal body docking in airway ciliated cells. Cby-/- mouse lung analysis, immunofluorescence, Foxj1 promoter analysis, electron microscopy PloS one High 21049041
2018 Centrosomal protein Dzip1l interacts with CBY1 (shown by co-immunoprecipitation), colocalizes with basal body appendage proteins, and acts upstream of CBY1 in ciliogenesis. Loss of Dzip1l reduces ciliogenesis and prevents removal of the capping protein Cp110 from distal mother centrioles, arresting ciliogenesis at the ciliary bud stage. Co-immunoprecipitation, Dzip1l knockout mouse, immunofluorescence, epistasis analysis Development Medium 29487109
2021 DZIP1 forms a multimeric complex with CBY1 and β-catenin at the basal body of primary cilia during cardiac valve development. A specific DZIP1 peptide is required for stabilization of this complex and suppression of β-catenin activities. Loss of DZIP1-CBY1 interaction leads to increased nuclear β-catenin, elevated MMP2, altered ECM, and myxomatous valve phenotype. Co-immunoprecipitation, decoy peptide experiments, immunofluorescence, TOPflash reporter assay, mouse cardiac valve analysis Developmental dynamics Medium 33811421
2015 In CML cells, CBY1 protein stability is reduced upon binding to 14-3-3σ, a process mediated by BCR-ABL1 tyrosine kinase and AKT phosphorylation of CBY1 at serine 20. JNK phosphorylation of 14-3-3σ at S186 promotes dissociation of CBY1 from 14-3-3σ. The ubiquitin-proteasome system reduces CBY1 stability via enhanced SUMOylation when CBY1 is bound to 14-3-3σ. Co-immunoprecipitation, site-directed mutagenesis, kinase inhibitor experiments, SUMOylation assay PloS one Medium 26147002
2020 Loss-of-function variants in CBY1 cause a ciliopathy with features of Joubert syndrome in humans. Patient fibroblasts show reduced ability to ciliate, increased ciliary length, and reduced levels of the ciliary proteins AHI1 and ARL13B. Depletion of Cby1 in zebrafish causes ciliopathy-related phenotypes. Human genetics (biallelic LOF variants), patient fibroblast immunofluorescence, zebrafish morpholino knockdown Human mutation High 33131181
2021 Loss of CBY1 in mice causes severe exocrine pancreatic atrophy with dilated ducts, reduction in cilia number and length, inflammatory infiltration, and defective zymogen granule secretion in acinar cells. CBY1-KO acinar cells show altered polarity and accumulate zymogen granules due to defective exocytosis. Cby1 knockout mouse, immunofluorescence, electron microscopy, ex vivo acini secretion assay Scientific reports High 34446743
2024 The Cby-Fam92 module (near the ciliary membrane) and the Cep131-Cep162 module (near the axoneme) cooperatively maintain Cep290 at the basal body and control the initiation of ciliogenesis. Concurrent deletion of members of both modules leads to complete loss of Cep290 from the basal body and blocks ciliogenesis at its initiation stage. Drosophila genetics (double mutants), immunofluorescence, epistasis analysis PLoS biology Medium 38442096
2025 The crystal structure (2.2 Å) of mouse FAM92A BAR domain reveals an antiparallel crescent-shaped homodimer. FAM92A BAR directly binds the N-terminal region of CBY1, and their respective dimerizations synergistically enhance binding affinity. Structure-guided mutagenesis identified residues critical for lipid binding on the concave surface and residues essential for dimerization. X-ray crystallography, structure-guided mutagenesis, co-immunoprecipitation, binding affinity measurements The Journal of biological chemistry High 40484380
2026 Rhotekin interacts with CBY1 and competes with β-catenin for binding to CBY1, thereby relieving CBY1's antagonistic effect on β-catenin and activating the canonical Wnt/β-catenin pathway to promote osteoblast differentiation. Rhotekin also activates the FAK/AKT signaling pathway. Co-immunoprecipitation, competition binding assay, overexpression/knockdown in mesenchymal progenitors, in vivo bone marrow silencing Cellular signalling Medium 42000008
2010 CBY1 interacts with multiple NBPF proteins via a coiled-coil region in NBPF that binds the coiled-coil domain in the C-terminal region of CBY1. CBY1 also interacts with clusterin. NBPF1, CBY1, and clusterin can be co-immunoprecipitated together, suggesting a tri-molecular complex, though NBPF interaction does not influence CBY1's Wnt repressor function. Yeast two-hybrid screen, co-immunoprecipitation, TOPflash reporter assay Experimental cell research Low 20096688

Source papers

Stage 0 corpus · 66 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2003 Chibby, a nuclear beta-catenin-associated antagonist of the Wnt/Wingless pathway. Nature 231 12712206
1983 Major effect on susceptibility to urethan-induced pulmonary adenoma by a single gene in BALB/cBy mice. Journal of the National Cancer Institute 118 6573537
2008 Chibby cooperates with 14-3-3 to regulate beta-catenin subcellular distribution and signaling activity. The Journal of cell biology 116 18573912
1999 Development and aging of primitive hematopoietic stem cells in BALB/cBy mice. Experimental hematology 88 10340409
2014 Chibby promotes ciliary vesicle formation and basal body docking during airway cell differentiation. The Journal of cell biology 80 25313408
2009 Inactivation of Chibby affects function of motile airway cilia. The Journal of cell biology 79 19364920
2000 Differences between C57BL/6 and BALB/cBy mice in mortality and virus replication after intranasal infection with neuroadapted Sindbis virus. Journal of virology 65 10846099
2012 Drosophila chibby is required for basal body formation and ciliogenesis but not for Wg signaling. The Journal of cell biology 54 22508513
2014 Cby1 promotes Ahi1 recruitment to a ring-shaped domain at the centriole-cilium interface and facilitates proper cilium formation and function. Molecular biology of the cell 52 25103236
2007 Chibby, an antagonist of the Wnt/beta-catenin pathway, facilitates cardiomyocyte differentiation of murine embryonic stem cells. Circulation 52 17261658
2006 TC1 (C8orf4) enhances the Wnt/beta-catenin pathway by relieving antagonistic activity of Chibby. Cancer research 52 16424001
2004 PIGEA-14, a novel coiled-coil protein affecting the intracellular distribution of polycystin-2. The Journal of biological chemistry 52 15194699
2007 Chibby promotes adipocyte differentiation through inhibition of beta-catenin signaling. Molecular and cellular biology 48 17403895
2018 Chibby suppresses aerobic glycolysis and proliferation of nasopharyngeal carcinoma via the Wnt/β-catenin-Lin28/let7-PDK1 cascade. Journal of experimental & clinical cancer research : CR 47 29764469
2009 Nuclear-cytoplasmic shuttling of Chibby controls beta-catenin signaling. Molecular biology of the cell 47 19940019
2016 BAR Domain-Containing FAM92 Proteins Interact with Chibby1 To Facilitate Ciliogenesis. Molecular and cellular biology 43 27528616
2009 Fine-tuning of nuclear-catenin by Chibby and 14-3-3. Cell cycle (Georgetown, Tex.) 37 19158508
1990 Effects of social isolation and the time of day on testosterone levels in plasma of C57BL/6By and BALB/cBy mice. Steroids 35 2326831
2012 A Wnt/beta-catenin pathway antagonist Chibby binds Cenexin at the distal end of mother centrioles and functions in primary cilia formation. PloS one 34 22911743
2008 Real-time quantitative PCR analysis of pediatric ependymomas identifies novel candidate genes including TPR at 1q25 and CHIBBY at 22q12-q13. Genes, chromosomes & cancer 31 18663750
2010 Altered lung morphogenesis, epithelial cell differentiation and mechanics in mice deficient in the Wnt/β-catenin antagonist Chibby. PloS one 30 21049041
2015 Structural Analysis of the 14-3-3ζ/Chibby Interaction Involved in Wnt/β-Catenin Signaling. PloS one 26 25909186
1999 Multidose streptozotocin induction of diabetes in BALB/cBy mice induces a T cell proliferation defect in thymocytes which is reversible by interleukin-4. Cellular immunology 26 10066341
2010 Chibby interacts with NBPF1 and clusterin, two candidate tumor suppressors linked to neuroblastoma. Experimental cell research 24 20096688
2007 The intrinsically disordered TC-1 interacts with Chibby via regions with high helical propensity. Protein science : a publication of the Protein Society 24 17905836
2018 Centrosomal protein Dzip1l binds Cby, promotes ciliary bud formation, and acts redundantly with Bromi to regulate ciliogenesis in the mouse. Development (Cambridge, England) 22 29487109
2006 Reduced expression of beta-catenin inhibitor Chibby in colon carcinoma cell lines. World journal of gastroenterology 21 16570344
2020 Loss of CBY1 results in a ciliopathy characterized by features of Joubert syndrome. Human mutation 20 33131181
2015 Chibby functions to preserve normal ciliary morphology through the regulation of intraflagellar transport in airway ciliated cells. Cell cycle (Georgetown, Tex.) 20 26266958
2011 Structural characterization of partially disordered human Chibby: insights into its function in the Wnt-signaling pathway. Biochemistry 20 21182262
1982 Molecular heterogeneity of D-end products detected by anti-H-2.28 sera. I. A. molecule similar to Qa-2, detected in the BALB/cBy but not in the BALB/c-H-2dm2 mutant. Immunogenetics 18 6179860
2021 A novel Lnc408 maintains breast cancer stem cell stemness by recruiting SP3 to suppress CBY1 transcription and increasing nuclear β-catenin levels. Cell death & disease 16 33934099
2009 Chibby forms a homodimer through a heptad repeat of leucine residues in its C-terminal coiled-coil motif. BMC molecular biology 16 19435523
2013 Chibby drives β catenin cytoplasmic accumulation leading to activation of the unfolded protein response in BCR-ABL1+ cells. Cellular signalling 15 23707389
2011 The expression patterns and correlations of chibby, β-catenin, and DNA methyltransferase-1 and their clinicopathological significance in lung cancers. APMIS : acta pathologica, microbiologica, et immunologica Scandinavica 14 21995627
2013 BCR-ABL1-associated reduction of beta catenin antagonist Chibby1 in chronic myeloid leukemia. PloS one 13 24339928
2005 Chibby, a novel antagonist of the Wnt pathway, is not involved in Wilms tumor development. Cancer letters 13 15737694
2012 Chibby suppresses growth of human SW480 colon adenocarcinoma cells through inhibition of β-catenin signaling. Journal of molecular signaling 12 22651859
2004 Is the gene encoding Chibby implicated as a tumour suppressor in colorectal cancer ? BMC cancer 11 15245581
2006 Differential Susceptibility of BALB/c and BALB/cBy mice to Graves' hyperthyroidism. Thyroid : official journal of the American Thyroid Association 9 16889488
2021 DZIP1 regulates mammalian cardiac valve development through a Cby1-β-catenin mechanism. Developmental dynamics : an official publication of the American Association of Anatomists 8 33811421
2020 Role of DZIP1-CBY-FAM92 transition zone complex in the basal body to membrane attachment and ciliary budding. Biochemical Society transactions 8 32491167
2015 14-3-3 Binding and Sumoylation Concur to the Down-Modulation of β-catenin Antagonist chibby 1 in Chronic Myeloid Leukemia. PloS one 8 26147002
2024 Cep131-Cep162 and Cby-Fam92 complexes cooperatively maintain Cep290 at the basal body and contribute to ciliogenesis initiation. PLoS biology 7 38442096
2015 DNA methyltransferase 1 drives transcriptional down-modulation of β catenin antagonist Chibby1 associated with the BCR-ABL1 gene of chronic myeloid leukemia. Journal of cellular biochemistry 7 25389112
2013 Phosphorylation of C-terminal polycystin-2 influences the interaction with PIGEA14: a QCM study based on solid supported membranes. Biochemical and biophysical research communications 7 23838289
2021 Loss of the ciliary protein Chibby1 in mice leads to exocrine pancreatic degeneration and pancreatitis. Scientific reports 6 34446743
2018 Cloning, identification and function analysis of a Chibby homolog from Litopenaeus vannamei. Fish & shellfish immunology 6 29689303
2017 Chibby 1: a new component of β-catenin-signaling in chronic myeloid leukemia. Oncotarget 6 29152155
2011 Generation and characterization of monoclonal antibodies against human Chibby protein. Hybridoma (2005) 6 21529289
2020 Combined Chibby and β-Catenin Predicts Clinical Outcomes in Patients with Hepatocellular Carcinoma. International journal of molecular sciences 5 32192213
2017 Chibby1 knockdown promotes mesenchymal-to-epithelial transition-like changes. Cell cycle (Georgetown, Tex.) 5 28107095
2016 Conformational characterization of the intrinsically disordered protein Chibby: Interplay between structural elements in target recognition. Protein science : a publication of the Protein Society 5 27082063
2015 Expression of CBY and methylation of CBY at promoter region in human laryngeal squamous cell carcinoma. Tumori 4 25838250
2024 Identification of a novel mutation in chibby family member 2 in a non-obstructive azoospermic patient. Reproductive biology 3 38733656
2018 Anti-oncogenic activity of Chibby in the development of human nasopharyngeal carcinoma. Oncology letters 3 29552214
2014 Downregulated Chibby in laryngeal squamous cell carcinoma with increased expression in laryngeal carcinoma Hep-2 cells. Oncology reports 3 25175341
2018 Chibby is a weak regulator of β-catenin activity in gastric epithelium. Journal of cellular physiology 2 30063079
2013 No important role for genetic variation in the Chibby gene in monogenic and complex obesity. Molecular biology reports 2 23645032
1999 The H-mshi antigen is conserved among standard BALB/cBy, C57BL/6J, and wild-derived CAST/Ei and SPRET/Ei inbred strains of mice. Immunogenetics 2 10369925
2023 Elimination of 4T1 Mammary Tumor Cells by BALB/cBy UBC-GFP Transgenics following Stable Inheritance of the H-2b MHC Allele. ImmunoHorizons 1 36637515
2023 Upregulated TC1 and downregulated Chibby were correlated with the aberrant β-catenin expression in laryngeal squamous cell carcinoma. Medicine 1 37986347
2022 Defective bone repletion in aged Balb/cBy mice was caused by impaired osteoblastic differentiation. Journal of bone and mineral metabolism 1 35947191
2017 Downregulation of nuclear and cytoplasmic Chibby is associated with advanced cervical cancer. Oncology letters 1 29181101
2026 Rhotekin contributes to osteoblast differentiation and bone homeostasis by interacting with Chibby 1. Cellular signalling 0 42000008
2025 Dimerization of the BAR domain-containing protein FAM92A modulates lipid binding and interaction with CBY1. The Journal of biological chemistry 0 40484380