| 2010 |
Cryo-EM structure of APC/C(Cdh1) bound to a D-box peptide at ~10 Å resolution revealed that Cdh1 and Apc10 together form a co-receptor for the D-box degron motif. Cdh1 repositions toward Apc10 within the central cavity of the APC/C, and NMR spectroscopy demonstrated direct D-box–Apc10 interactions, establishing that Apc10 directly contributes to D-box recognition alongside the co-activator. |
Single-particle cryo-EM, difference mapping, NMR spectroscopy |
Nature |
High |
21107322
|
| 2001 |
Crystal structure of human APC10/DOC1 at 1.6 Å resolution revealed a beta-sandwich jellyroll fold homologous to ligand-binding domains of galactose oxidase and coagulation factor Va. Biochemical experiments further demonstrated that the C-terminus of APC10 directly binds CDC27/APC3, a TPR-repeat-containing APC subunit. |
X-ray crystallography (1.6 Å); biochemical binding assay (C-terminus of APC10 binding to CDC27/APC3) |
Nature structural biology |
High |
11524682
|
| 2002 |
Crystal structure of S. cerevisiae Doc1/Apc10 at 2.2 Å resolution showed a beta-sandwich homologous to the galactose-binding domain of galactose oxidase, the C2 domain of coagulation factor, and XRCC1. Residues invariant across Doc1/Apc10 sequences, including a temperature-sensitive mitotic arrest mutant, map to a beta-sheet region proposed to mediate biomolecular interactions and APC ubiquitination function. |
X-ray crystallography (2.2 Å); comparative structural analysis with mutagenesis data mapping |
Journal of molecular biology |
High |
11884135
|
| 1999 |
Doc1/Apc10 was shown to be a stoichiometric subunit of the yeast APC throughout the cell cycle. Mutation of Doc1/Apc10 inactivates APC ubiquitination activity without destabilizing the complex. The orthologous human APC10 protein is also a genuine APC subunit in vertebrates (human and frog), and its cellular levels and APC association are not cell-cycle-regulated, as determined by biochemical fractionation and mass spectrometric analysis. |
Immunoprecipitation, biochemical fractionation, mass spectrometry, in vivo ubiquitination assays |
The Journal of biological chemistry |
High |
10318877
|
| 1998 |
In fission yeast, apc10+ is essential for viability and required for ubiquitination and degradation of mitotic B-type cyclins. apc10 mutants show temperature-sensitive growth with defects in chromosome segregation and fail to arrest at G1 upon nitrogen starvation. A subpopulation of Apc10 co-immunoprecipitates with the APC, though it does not co-sediment with the 20S complex, suggesting a regulatory association. |
Genetic mutant analysis, co-immunoprecipitation, cell cycle analysis, ubiquitination assay |
The EMBO journal |
High |
9736616
|
| 1999 |
Human APC10/Doc1 binds APC core subunits throughout the cell cycle and localizes to centrosomes and mitotic spindles during mitosis, to kinetochores from prophase to anaphase, and to the midbody during telophase/cytokinesis, as determined by co-immunoprecipitation and immunofluorescence localization studies. |
Co-immunoprecipitation; immunofluorescence microscopy (subcellular localization) |
Oncogene |
Medium |
10498862
|
| 2004 |
ANAPC10 physically interacts with Smad3 (via the MH2 domain), and together with CDH1 forms a complex with HEF1 (NEDD9). Domain mapping showed distinct Smad3 MH2 subdomains bind APC10 and HEF1. Overexpression of APC10 and CDH1 regulated HEF1 protein levels, suggesting Smad3 recruits the APC/C to HEF1 for ubiquitination and proteasomal degradation via direct Smad3–APC10 interaction. |
Co-immunoprecipitation, domain mapping, overexpression/protein level assay |
BMC cell biology |
Medium |
15144564
|
| 2019 |
The pseudosubstrate APC/C inhibitor Acm1 from budding yeast suppresses APC/C activity by combining high-affinity Cdh1 binding with a C-terminal D-box extension that specifically disrupts the normal interaction with Doc1/Apc10, thereby perturbing reaction processivity in ubiquitylation. Mutation of the conserved D-box converted Acm1 into an ABBA-motif-dependent APC/CCdh1 substrate, and biochemical analysis confirmed the extension's role in inhibiting processivity via Doc1/Apc10. |
In vivo mutant analysis, biochemical APC/C activity assays, site-directed mutagenesis |
The Journal of biological chemistry |
Medium |
31562243
|
| 2001 |
Disruption of the mouse Apc10/Doc1 gene underlies the oligosyndactylism (Os) radiation-induced mutation and two transgene-induced alleles (94-A and 94-K), all exhibiting a cell-autonomous block in metaphase-to-anaphase transition, establishing that Apc10/Doc1 is required for this cell cycle transition in vivo. |
Genetic mapping, molecular characterization of three mutant alleles, cell cycle phenotype analysis |
Genomics |
Medium |
11247669
|
| 2007 |
In Drosophila, loss-of-function mutations in Apc10/Doc1 cause metaphase-like arrest, chromosome overcondensation, high mitotic index, and accumulation of cyclin B (an APC/C substrate) in larval neuroblasts, establishing that Apc10/Doc1 is essential for APC/C E3 ubiquitin ligase activity and cyclin B ubiquitination in vivo. |
Genetic loss-of-function (mutant alleles), immunostaining for cyclin B, mitotic index quantification |
Acta biologica Hungarica |
Medium |
18297794
|
| 2021 |
During interphase, APC10 interacts with NLRP3 and promotes NLRP3 inflammasome activation; during mitosis, APC10 dissociates from NLRP3 to repress inflammatory responses, establishing a cell-cycle-dependent switch role for APC10 in innate immune signaling. |
Co-immunoprecipitation, cell cycle stage-specific analysis, inflammasome activation assays |
FEBS letters |
Medium |
34407203
|
| 2012 |
ANAPC10 protein is mainly expressed in the cytoplasm of spermatogonia and leptotene/pachytene spermatocytes in the developing mouse testis, as established by immunofluorescence and in situ hybridization. |
In situ hybridization, immunofluorescence microscopy |
Biology of reproduction |
Low |
22190705
|