| 2014 |
Drosophila YETI (ortholog of CFDP1) binds to polytene chromosomes through its conserved BCNT domain, physically interacts with histone variant H2A.V, HP1a, and the ATPase subunit Domino-A (DOM-A) of the DOM/Tip60 chromatin remodeling complex, and is required for H2A.V accumulation at chromatin sites. Loss of YETI causes lethality and severe defects in higher-order chromatin organization including impaired association of H2A.V, nucleosomal histones, and epigenetic marks with polytene chromosomes. YETI was identified as a downstream target of DOM-A. |
Co-immunoprecipitation, chromatin binding assays, RNAi/genetic loss-of-function, immunostaining of polytene chromosomes |
Journal of cell science |
High |
24652835
|
| 2017 |
Human CFDP1 binds to chromatin and interacts with subunits of the SRCAP chromatin remodeling complex. RNAi-mediated depletion of CFDP1 in HeLa cells causes chromosome organization defects, impaired SMC2 condensin recruitment, and cell cycle progression defects. |
RNAi knockdown, Co-immunoprecipitation, chromatin fractionation, immunofluorescence, cell cycle analysis |
Scientific reports |
High |
28367969
|
| 2016 |
Both Drosophila YETI and human CFDP1 undergo homodimerization mediated by the BCNT domain. YETI and CFDP1 physically interact with each other to form inactive heterodimers, which underlies the dominant-negative effect of CFDP1 expression in flies. |
GST pull-down assays, in vivo expression in Drosophila with phenotypic analysis |
Scientific reports |
Medium |
27151176
|
| 2003 |
Drosophila YETI (CFDP1 ortholog) binds specifically to both the kinesin light chain (via tetratricopeptide repeats) and the kinesin heavy chain (amino acids 675–975) subunits of kinesin-I, as shown by yeast two-hybrid and copurification from S2 cells. YETI localizes to both nucleus and cytosol. |
Yeast two-hybrid screen, copurification assay from Drosophila S2 cells, immunostaining |
Biology of the cell |
Medium |
14720462
|
| 2015 |
Mammalian Bcnt/Cfdp1 has an acidic stretch in its disordered N-terminal region that causes anomalous gel mobility on SDS-PAGE. Ser250 in the conserved BCNT-C domain is heavily phosphorylated in vivo and is a major determinant of the protein's electrophoretic behavior. Four lysine residues including Lys268 in BCNT-C are acetylated in vivo, and Bcnt/Cfdp1 is acetylated in vitro by CREB-binding protein (CBP). Bovine and human BCNTs are phosphorylated by casein kinase II in vitro. |
Deletion mutant expression in E. coli and HEK cells, phosphatase treatment, Ser250 substitution mutagenesis, mass spectrometry-based phosphosite mapping, in vitro acetylation assay with CBP |
Bioscience reports |
High |
26182435
|
| 1999 |
Bovine BCNT (Cfdp1 ortholog) shows partial nuclear localization as determined by subcellular fractionation and immunohistochemistry in bovine epithelial cells and brain tissue, with a significant nuclear fraction and a major cytosolic portion. Bovine BCNT is a phosphoprotein, and both bovine and human BCNTs are phosphorylated by casein kinase II in vitro. |
Subcellular fractionation, immunohistochemistry, in vitro kinase assay with casein kinase II |
Biochimica et biophysica acta |
Medium |
10350657
|
| 2024 |
CFDP1 colocalizes with heterochromatin at major and minor satellite repeats and is essential for structural stability of centromeric heterochromatin including CENPA, HP1α, and H2A.Z. Loss of CFDP1 reduces RCC1 binding to satellite repeats, decreasing RanGTP levels and impairing chromatin-mediated microtubule nucleation at the onset of mitotic spindle formation. Knockdown of histone chaperone ANP32E in CFDP1-deficient cells/mice partially rescued H2A.Z levels, RanGTP, craniofacial defects, and microtubule nucleation. |
Co-localization imaging, ChIP, RanGTP activity assays, genetic rescue experiments (ANP32E knockdown in CFDP1 KO cells and mice), microtubule nucleation assays |
PLoS biology |
High |
38630655
|
| 2025 |
CFDP1 weakly associates with the human SRCAP complex (SRCAP-C) in a salt-concentration-dependent manner. SRCAP-C purified under high-salt conditions lacks CFDP1 and is inactive for H2A.Z dimer exchange; addition of exogenous CFDP1 restores H2A.Z deposition activity of SRCAP-C. CFDP1 stimulates the basal ATPase activity of reconstituted SRCAP-C. CFDP1 deficiency in hiPSCs causes genome-wide reduction of H2A.Z, H3K27me3, and H3K4me3 deposition and upregulation of developmental genes normally marked by these modifications. |
Biochemical reconstitution of SRCAP-C, in vitro H2A.Z dimer exchange assay, ATPase activity assay, CFDP1 KO in hiPSCs with ChIP-seq |
bioRxivpreprint |
High |
41278978
|
| 2026 |
CFDP1 functions as a bipartite microtubule-associated protein (MAP): its acidic N-terminus harbors a nuclear localization signal required for dissociation of importin α from the spindle assembly factor TPX2 (thereby promoting Aurora A kinase activation and microtubule nucleation), while its basic C-terminus interacts with tubulin, co-localizes with the mitotic spindle, and promotes microtubule bundling and polymerization. Loss of CFDP1 in mice causes gastrulation defects and embryonic lethality at e8.5 associated with chromosome segregation spindle defects and loss of K-fiber stability. |
Mouse CFDP1 knockout (phenotypic analysis), domain dissection with N-terminal/C-terminal constructs, importin α–TPX2 dissociation assay, tubulin-binding assay, microtubule bundling/polymerization assay, co-localization with mitotic spindle |
International journal of molecular sciences |
High |
41683788
|
| 2021 |
In zebrafish, loss of Cfdp1 (cfdp1 mutants) causes G2-to-M phase cell cycle delay, mitotic block before anaphase (despite normal spindle formation), increased apoptosis (via tp53-dependent pathway), and failure of neural progenitor differentiation in the cerebellum and retina, accompanied by elevated cyclin B1 expression. |
Zebrafish cfdp1 mutant analysis, phospho-histone H3 staining, apoptosis assays, tp53 inhibition rescue, cyclin B1 expression analysis |
Developmental dynamics |
Medium |
33987914
|
| 2023 |
In zebrafish, cfdp1 loss-of-function (morpholino knockdown and CRISPR knockout) causes arrhythmic hearts with defective cardiac performance and lethality. Mechanistically, cfdp1 abrogation downregulates Wnt signaling in embryonic hearts during valve development without affecting Notch activation. |
Morpholino knockdown, CRISPR knockout in zebrafish, cardiac function imaging, Wnt and Notch pathway reporter/expression analysis |
Cells |
Medium |
37566073
|
| 2022 |
CFDP1 promotes hepatocellular carcinoma malignancy via NEDD4-mediated ubiquitination and degradation of PTEN, leading to activation of the PI3K/AKT signaling pathway, as demonstrated by western blotting in HCC cell lines and in vivo tumor models. |
Western blotting, in vitro and in vivo loss/gain-of-function experiments in HCC cells, GSEA/GeneCards pathway analysis, xenograft mouse model |
Cancer medicine |
Low |
35861040
|
| 2012 |
TFII-I transcription factors (GTF2I/GTF2IRD1) are directly recruited to the promoter of CFDP1 in human neural crest progenitor cells, identifying CFDP1 as a direct transcriptional target of TFII-I. |
ChIP-chip (chromatin immunoprecipitation with tiling promoter arrays) in human neural crest progenitor cells |
The Cleft palate-craniofacial journal |
Medium |
23145914
|
| 2025 |
In C2C12 myoblasts, fluorescent protein-tagged Bcnt/Cfdp1 localizes predominantly to the nucleus, preferentially in low-DAPI-density regions, and this localization persists in differentiated myotubes. However, detergent-based biochemical fractionation consistently recovers a substantial fraction in the cytoplasm, an artifact attributed to the elastic/disordered properties of Bcnt/Cfdp1 causing artifactual translocation during fractionation under macromolecular crowding conditions. |
Live-cell fluorescence imaging of tagged Bcnt/Cfdp1, detergent-based subcellular fractionation, digitonin-based fractionation, quantitative proteomics (LC-MS/MS) of fractions |
bioRxivpreprint |
Medium |
bio_10.1101_2025.04.28.651124
|