| 1998 |
ANAPC5 (APC5) was identified as one of four previously uncharacterized subunits of the anaphase-promoting complex (APC/C), an eight-subunit E3 ubiquitin ligase that targets cell cycle regulators for degradation; APC5 shares no similarity to proteins of known function but is a core structural component of the complex. |
Biochemical purification and cloning of human APC subunits |
Science |
High |
9469815
|
| 2003 |
APC5, together with APC1 and APC4, forms a scaffold subcomplex that connects the catalytic module (APC2/APC11) with the TPR subunits; this subcomplex can assemble multiubiquitin chains but cannot bind the co-activator CDH1 or ubiquitinate substrates alone. |
Biochemical fractionation and reconstitution of human APC subcomplexes; in vitro ubiquitination assays; CDH1 binding assays |
Current Biology |
High |
12956947
|
| 2011 |
Cryo-EM combined with mass spectrometry and crystallographic docking defined APC5 as a scaffolding subunit that, together with APC1 and APC4 (the platform subcomplex), coordinates juxtaposition of the catalytic module (APC2/APC11/APC10) and the TPR subcomplex (CDC16/CDC23/CDC27) within the APC/C. |
Electron microscopy, mass spectrometry, recombinant reconstitution of holo-APC/C, and docking of crystallographic coordinates |
Nature |
High |
21307936
|
| 2015 |
Crystal structure of the N-terminal domain of human APC5 (Apc5N) was determined, revealing an α-helical fold; in the context of the APC/C cryo-EM map, Apc5N shows small conformational changes and regions of Apc4 disordered in crystal gain order through contacts with Apc5. |
X-ray crystallography of Apc5N and Apc4; fitting into 3.6-Å cryo-EM map of APC/C |
Journal of Molecular Biology |
High |
26343760
|
| 2016 |
APC5 is part of the platform subcomplex (Apc1/Apc4/Apc5/Apc15); deletion of the Apc1 WD40 domain locks the APC/C into an inactive conformation, implicating the platform in the coactivator-induced allosteric transition that allows UbcH10 binding and substrate ubiquitination initiation. |
Crystal structure of Apc1N, cryo-EM of mutant APC/C-Cdh1 complex lacking Apc1(WD40), in vitro ubiquitination assays |
PNAS |
High |
27601667
|
| 2005 |
APC5 and APC7 directly interact with the transcriptional co-activators CBP and p300 through evolutionarily conserved protein-protein interaction domains (shared with adenovirus E1A); this interaction stimulates CBP/p300 acetyltransferase activity and potentiates CBP/p300-dependent transcription. APC5 and APC7 suppress E1A-mediated transformation in a CBP/p300-dependent manner. |
Co-immunoprecipitation, GST pulldown, acetyltransferase activity assays, reporter gene assays, siRNA knockdown, focus formation assay |
Nature |
High |
16319895
|
| 2004 |
APC5 (Apc5) binds poly(A) binding protein (PABP) and represses IRES-mediated translation of PDGF-2 mRNA; APC5 overexpression counteracts PABP-stimulated IRES activity, and APC5 is degraded upon megakaryocytic differentiation in correlation with IRES activation. |
Yeast three-hybrid screen, co-immunoprecipitation, sucrose gradient sedimentation with ribosomal fraction, IRES reporter assays, differentiation experiments |
Molecular and Cellular Biology |
Medium |
15082755
|
| 2013 |
APC5 (AnapC5) interacts with both IL-17RA and IL-17RC receptor subunits and with the negative regulator A20 (TNFAIP3); siRNA silencing of AnapC5 enhanced IL-17-induced gene expression, identifying AnapC5 as an inhibitory adaptor in IL-17 signaling distinct from the Itch/TAXBP1 scaffold used in TNFα/IL-1 pathways. |
Yeast 2-hybrid screen, siRNA knockdown, co-immunoprecipitation, IL-17-responsive reporter gene assays |
PLoS One |
Medium |
23922952
|
| 2012 |
APC5 binds E2F1 (identified by Co-IP in vivo and GST pulldown in vitro) and is essential for APC/C(Cdh1)-mediated K11-linked ubiquitination and proteasomal degradation of E2F1 after S phase. |
Co-immunoprecipitation, GST pulldown, ubiquitination assays with K11-specific ubiquitin, siRNA knockdown, proteasome inhibitor experiments |
Cell Cycle |
Medium |
22580462
|
| 2010 |
During HCMV infection of quiescent cells, APC5 and APC4 are degraded in a proteasome-dependent manner, temporally associated with APC/C disassembly; immediate early viral gene expression is not sufficient, implicating early viral gene products in APC5 degradation. |
Immunoblot, proteasome inhibitor treatment, mutant virus infection (ΔUL97), mass spectrometry analysis of Cdh1 phosphorylation |
Journal of Virology |
Medium |
20686030
|
| 2012 |
HCMV protein pUL21a binds the APC/C and is necessary and sufficient for proteasome-dependent degradation of APC5 and APC4 subunits, causing APC/C disruption; residues P109-R110 of pUL21a are critical for APC binding and regulation. |
Proteomics/MS, Co-IP, siRNA knockdown, point mutant virus construction, ubiquitin ligase activity assays |
PLoS Pathogens |
High |
22792066
|
| 2015 |
A cellular mechanism exists whereby depletion of any one of APC1, APC4, APC5, or APC8 leads to co-dependent downmodulation of all three platform subunits (APC1, APC4, APC5); this inter-dependency was demonstrated in uninfected cells independent of viral infection. |
siRNA knockdown of individual APC subunits, immunoblot quantification of co-depletion |
Journal of Virology |
Medium |
25903336
|
| 2002 |
In Drosophila, IDA (the APC5 ortholog) is required for APC/C function in imaginal disc cell proliferation; ida mutants show high mitotic index, aneuploid chromosomes, and failure to degrade cyclin B, but some APC/C substrates controlling sister-chromatid separation are still turned over, suggesting APC5 controls specific regulatory subfunctions of the APC/C. |
Genetic cloning and characterization, immunofluorescence cytology, cyclin B immunostaining in mutant brains |
Journal of Cell Science |
High |
11870214
|
| 2003 |
In budding yeast, Mnd2 and Swm1 (novel APC subunits) interact directly with Apc5 (and Cdc23/Apc1) when coexpressed in vitro, placing Apc5 as a docking site for these peripheral APC subunits. |
Mass spectrometry of purified APC, in vitro transcription/translation co-immunoprecipitation, epitope-tagging co-purification |
Journal of Biological Chemistry |
Medium |
12609981
|
| 2009 |
In fission yeast, transcription factor Atf1 physically binds the APC/C in vivo and addition of purified Atf1 to a cell-free system stimulates APC/C-dependent ubiquitylation of cyclin B and securin; Atf1 suppresses the mitotic arrest of the apc5-1 mutant in a bZIP-domain-independent manner. |
Genetic suppressor screen, co-immunoprecipitation, cell-free ubiquitination assay with purified Atf1 |
Journal of Biological Chemistry |
Medium |
19584054
|
| 2002 |
In yeast, APC5 (RMC1) is required for in vitro chromatin assembly; the rmc1/apc5 allele genetically interacts with apc9Δ, apc10Δ, and cdc26Δ, and confers UV sensitivity, plasmid loss, and G2/M accumulation, establishing APC5 as required for APC-dependent chromatin assembly and genomic stability. |
In vitro chromatin assembly screen, genetic interaction analysis, cell cycle FACS, UV survival assays |
Genetics |
Medium |
12399376
|
| 2013 |
In yeast, Apc5 (used as two-hybrid bait) interacts with the lifespan determinant Fob1; Fob1 is unstable in G1 and stabilized in apc5(CA) and rpn10 (proteasome) mutants, and a putative L-box destruction motif in Fob1 is required for its modifications, placing Fob1 as an APC/C substrate that influences rDNA stability and replicative lifespan. |
Yeast two-hybrid, protein stability assays (cycloheximide chase), mutant analysis (apc5CA, rpn10), lifespan assays, rDNA recombination assays |
Genetics |
Medium |
24361936
|
| 2025 |
ANAPC5 mediates ubiquitination of GPAA1 (a catalytic subunit of GPI transamidase); radiation inhibits the APC/C complex, reducing ANAPC5-mediated ubiquitination of GPAA1, leading to GPAA1 accumulation, enhanced GPI anchoring of CD24, increased surface CD24 expression, and tumor immune evasion. |
Co-immunoprecipitation, ubiquitination assays, GPAA1 and CD24 expression analysis in irradiated cells, GPAA1/CD24 ablation in preclinical tumor models, flow cytometry |
Cancer Research |
Medium |
41512182
|
| 2025 |
ANAPC5 overexpression inhibits M1 macrophage polarization and promotes M2 polarization in LPS-induced acute lung injury by inducing ubiquitination of EGFR, reducing EGFR activation and expression; EGFR knockdown reversed the inhibitory effects of ANAPC5 on inflammation, and EGFR suppressed CD24 expression downstream, placing ANAPC5 as a negative regulator of EGFR/CD24-axis-mediated macrophage polarization. |
ANAPC5 overexpression in vivo (ALI mouse model) and in vitro (macrophages), ubiquitination assays for EGFR, cytokine measurement, macrophage polarization markers, rescue experiments with EGFR |
Cellular Immunology |
Medium |
40834712
|
| 2024 |
In mouse and human cell line models, co-depletion of ANAPC5 (APC5) exacerbates mitotic arrest induced by KIF18A depletion, while co-depletion of ANAPC7 partially rescues it, revealing that ANAPC5 and ANAPC7 have opposing effects on APC/C activity during mitosis and modulate sensitivity to KIF18A loss. |
siRNA co-depletion experiments in cell lines, time-lapse mitotic progression assays, mouse genetic screen for loci modifying KIF18A-dependent germ cell depletion |
Scientific Reports / bioRxiv |
Medium |
39677807 40596695
|
| 2007 |
In C. elegans, a mutation in the APC5-like component SUCH-1/APC5 delays anaphase onset in germline and early embryonic cells and acts as a suppressor of mdf-1/MAD1 (spindle assembly checkpoint) lethality by delaying mitotic progression with concomitant IFY-1/securin accumulation. |
EMS mutagenesis screen, time-lapse imaging of embryonic cells, IFY-1 immunostaining, genetic suppression analysis |
Genetics |
Medium |
17237515
|
| 2010 |
In C. elegans, the two APC5 paralogs SUCH-1 and GFI-3 are co-expressed in germline but have non-overlapping expression in other tissues; single depletion has no meiotic effect, but co-depletion causes meiotic arrest, demonstrating redundant APC5 function during meiotic divisions. |
RNAi co-depletion, meiotic phenotype scoring, expression pattern analysis |
Genetics |
Medium |
20944012
|
| 2010 |
In C. elegans, a novel allele of SUCH-1/APC5 causes prolonged mitosis that is dependent on the spindle assembly checkpoint (SAC); inactivation of SAC components MDF-1/MAD1 or MDF-2/MAD2 rescues mitotic timing in APC/C-compromised embryos assembling monopolar spindles, indicating mutual antagonism between APC/C (via APC5) and the SAC. |
Genetic characterization of such-1(t1668) allele, SAC component RNAi, time-lapse imaging of mitotic duration |
Genetics |
Medium |
20944014
|