| 2005 |
ODF2 is indispensable for the formation of distal/subdistal appendages on mother centrioles and for the generation of primary cilia. In Odf2−/− mouse F9 cells, both distal and subdistal appendages disappear from mother centrioles, and primary cilia formation is completely suppressed; these defects are rescued by exogenous Odf2 expression. |
Knockout cell line (Odf2−/− F9 cells), immunofluorescence, ultrathin-section electron microscopy, rescue by exogenous expression |
Nature cell biology |
High |
15852003
|
| 2012 |
Odf2 is required for basal foot formation on basal bodies of ciliated epithelia; loss of basal feet disrupts polarized alignment of basal bodies and coordinated ciliary beating, without affecting planar cell polarity or ciliogenesis per se. The C-terminal region of Odf2 (encoded by exons 6–7) is specifically required for basal foot formation. |
Conditional knockout mice (Odf2 ΔEx6,7/ΔEx6,7), phenotypic analysis of tracheal cilia beating, electron microscopy, immunofluorescence |
Cell |
High |
22265411
|
| 1997 |
ODF2 (Odf84) interacts with the outer dense fiber protein ODF1 (Odf27) via leucine zippers; all leucine residues in the upstream leucine zipper of ODF2 are required for this interaction. ODF2 contains two C-terminal leucine zippers and localizes to outer dense fibers by fluorescence and immunoelectron microscopy. |
Yeast two-hybrid screen using Odf27 leucine zipper as bait, leucine-to-alanine mutagenesis, immunofluorescence, immunoelectron microscopy |
The Journal of biological chemistry |
High |
9045620
|
| 2009 |
The hCenexin1 splice variant (but not hODF2 itself) localizes to somatic centrosomes via its variant-specific C-terminal extension. The C-terminal extension contains a Cdc2-phosphorylated S796 motif that recruits Plk1; this Plk1 interaction is required for proper recruitment of pericentrin and gamma-tubulin and for bipolar spindle formation. Earlier in the cell cycle, hCenexin1 recruits ninein and promotes primary cilia formation independently of Plk1. |
Expression of hODF2 vs. hCenexin1 constructs and deletion mutants in cells, Co-IP/interaction assays, immunofluorescence, phospho-mutant analysis (S796A), spindle phenotype analysis |
Developmental cell |
High |
19386263
|
| 2013 |
Distinct domains of ODF2/cenexin are required for different appendage types: amino acids 188–806 are required for ciliogenesis and transition fiber (distal appendage) formation, whereas aa 1–59 combined with aa 188–806 are additionally required for basal foot (subdistal appendage) formation. Transition fibers/distal appendages are required for ciliogenesis, while subdistal appendages stabilize centrosomal microtubules. |
Odf2-knockout F9 cells rescued with Odf2 deletion constructs, electron microscopy, immunofluorescence, microtubule stability assays |
The Journal of cell biology |
High |
24189274
|
| 2004 |
ODF2 is a self-interacting protein that forms fibrillar structures in vivo and associates with microtubules in vitro (microtubule cosedimentation and coprecipitation). However, direct interaction with tubulin alone was not detected, suggesting the microtubule association is mediated by additional proteins. |
GFP-fusion expression in mammalian cells, in vitro microtubule cosedimentation, coprecipitation assay |
Journal of cell science |
Medium |
15340007
|
| 2011 |
Trichoplein binds both Odf2 and ninein at the centrosome. Odf2 depletion inhibits trichoplein recruitment to the mother centriole subdistal region, whereas ninein depletion does not, placing Odf2 upstream of trichoplein in the hierarchical assembly. Trichoplein depletion abolishes ninein but not Odf2 recruitment, and depletion of each impairs microtubule anchoring at the centrosome. |
Co-immunoprecipitation, siRNA knockdown, immunocytochemistry, microtubule anchoring assay |
Journal of cell science |
Medium |
21325031
|
| 2008 |
A peptide of 42 amino acids specific to the Cenexin isoform (encoded by exon 3b) is necessary for targeting ODF2/Cenexin to the centrosome and primary cilia. The C-terminal coiled-coil region of ODF2 also contributes to centrosomal/ciliary targeting, presumably via self-association. Centrosomal targeting does not depend on dynein-mediated transport. |
Series of GFP-tagged deletion constructs transfected into NIH3T3 cells, immunofluorescence localization, dynein inhibition experiment |
European journal of cell biology |
Medium |
18171590
|
| 2013 |
Cenexin1 (ODF2 isoform 9), but not ODF2, is necessary and sufficient for primary cilia assembly in odf2−/− cells. Cenexin1 interacts with GTP-loaded Rab8a and localizes to distal/subdistal appendages, facilitating recruitment of the centriolar component Chibby, which is important for ciliogenesis. ODF2 localizes along the ciliary axoneme but does not support ciliogenesis. |
Rescue experiments in odf2−/− cells expressing ODF2 or Cenexin1, Co-IP (Rab8a interaction), immunofluorescence, Chibby recruitment assay |
Cell cycle |
Medium |
23343771
|
| 2016 |
Testis-specific serine/threonine kinase 4 (Tssk4) phosphorylates ODF2 at serine 76. The C-terminal region (aa 214–638) of Odf2 is required for its association with Tssk4. Phosphorylation at S76 was confirmed in vivo in mouse sperm by phospho-specific antibody and LC-MS/MS. |
Co-immunoprecipitation (Tssk4–Odf2 interaction), Ser/Thr/Lys-to-Ala point mutagenesis, in vivo phosphorylation confirmed by phospho-specific antibody and LC-MS/MS |
Scientific reports |
Medium |
26961893
|
| 2019 |
Cep128 associates with Odf2 (confirmed by co-immunoprecipitation) and is required for subdistal appendage (SDA) assembly downstream of Odf2. Cep128 knockdown causes dissociation of SDA components (centriolin, Ndel1, ninein, Cep170) from the centriole while Odf2 and distal appendage components remain; Cep128 KD also decreases centriolar microtubule stability. |
Super-resolution structured illumination microscopy (SR-SIM), co-immunoprecipitation, siRNA knockdown, immunofluorescence |
Genes to cells |
Medium |
30623524
|
| 2018 |
ODF2 maintains centrosome cohesion by restricting β-catenin accumulation at the centrosome. Depletion of ODF2 causes premature centrosome splitting and formation of tripolar spindles, associated with elevated centrosomal β-catenin levels. |
siRNA depletion of ODF2 in cultured cells, immunofluorescence for centrosome number and β-catenin localization, spindle analysis |
Journal of cell science |
Medium |
30257984
|
| 2014 |
Transcription factor Pax6 directly regulates Odf2 gene activity. In Pax6-deficient cortex (Sey/Sey mutant), mother centriole appendages are lost, RGCs fail to form primary cilia and detach from the ventricular surface, impairing interkinetic nuclear migration. Mechanistically, Pax6 acts upstream of Odf2 to control centriole maturation in cortical progenitors. |
Pax6-deficient mouse mutant (Sey/Sey), promoter reporter assay for Odf2 transcription, immunofluorescence of centrosomal appendages and cilia, interkinetic nuclear migration analysis |
Cellular and molecular life sciences |
Medium |
25352170
|
| 2019 |
CCDC42 interacts with ODF2 (and ODF1) in the formation of the spermatid cytoskeleton. CCDC42 localizes to the manchette, head-to-tail coupling apparatus (HTCA), and sperm tail in spermatids, and also to the centrosome in somatic cells. |
Co-immunoprecipitation (CCDC42 with ODF2 and ODF1), immunofluorescence in spermatids and somatic cells |
Frontiers in cell and developmental biology |
Low |
31475146
|
| 2013 |
Odf2/Cenexin transcription is repressed in cycling cells but upregulated in quiescent cells. C/EBPα, c-Jun, and the JNK pathway activator MEKK1 can enhance Odf2 transcription in cycling cells. Neither Rfx3, Foxj1, nor other predicted transcription factors activate Odf2 transcription. |
Promoter-reporter (luciferase) assays, co-expression of transcription factors, qRT-PCR |
Biochimica et biophysica acta |
Low |
23458833
|
| 2022 |
FOXA1 is a transcriptional activator of Odf2/Cenexin. FOXA1 binds the Odf2 promoter (confirmed by ChIP), its knockdown decreases ODF2 protein levels and impairs primary cilia formation. |
Reporter gene assay, qRT-PCR, Western blot, ChIP, siRNA knockdown of FOXA1 with cilia formation assay |
Scientific reports |
Medium |
36509813
|
| 2023 |
ODF2 negatively regulates CP110 levels at centrioles/basal bodies to control primary cilia formation. Knockdown of ODF2 increases CP110 levels, while ODF2 overexpression alone is insufficient to promote ciliogenesis. Co-expression of ODF2 with HYLS1 produces tube-like structures, suggesting ODF2 acts as a scaffold for NEURL4 or HYLS1 to mediate CP110 degradation. |
siRNA knockdown of ODF2, overexpression experiments, rapamycin-mediated dimerization for targeted centriolar recruitment, immunofluorescence for CP110 levels and cilia |
Cells |
Medium |
37681926
|
| 2025 |
In Xenopus, Odf2 localizes to the basal foot of basal bodies in multiciliated cells (MCCs). Morpholino-mediated knockdown of Odf2 impairs basal foot morphogenesis, reduces microtubule nucleation rate from basal bodies, causes cilia disorientation and reduced beating. Additionally, Odf2 is required for MCC motility and homotypic repulsion prior to surface emergence, with reduced migration speed altering MCC spacing. |
Morpholino knockdown in Xenopus embryo epidermis, electron microscopy, live imaging of basal body polarization and cilia beating, mathematical simulation of MCC spacing |
Developmental biology |
Medium |
39864486
|