CEP152

Summary: CEP152 performs its centriole-duplication scaffold function at centrosomes.

Reason: The preserved IBA follows the PAINT IBD at PTN000818649, recovered in the fixed-main PTHR10337 PAINT record. Human O94986 is legitimate descendant experimental evidence, alongside MGI:2139083; this is not circular transfer. Direct human scaffold, localization and depletion/rescue experiments agree with the inherited function. The detailed ancestral reconstruction was not independently repeated.

Summary: CEP152 performs its centriole-duplication scaffold function at centrosomes.

Reason: The preserved IBA follows the PAINT IBD at PTN000818649, recovered in the fixed-main PTHR10337 PAINT record. Human O94986 is legitimate descendant experimental evidence, alongside MGI:2139083; this is not circular transfer. Direct human scaffold, localization and depletion/rescue experiments agree with the inherited function. The detailed ancestral reconstruction was not independently repeated.

Summary: Centrosomal localization is an established part of CEP152 function.

Reason: The original UniProt subcellular-location mapping is retained. Endogenous and expressed human CEP152 localize at centrosomes in multiple primary studies; the current HPA record independently calls centrosomal staining supported. The refreshed GOA uses a different electronic source chain, which does not replace this frozen original assertion.

Summary: CEP152 forms a peripheral scaffold around the proximal region of centrioles.

Reason: Human microscopy places CEP152 around the centriole rather than within its lumen. This supports the broad centriolar location while the PCM term describes its finer structural context.

Summary: Human CEP152 associates with PLK4.

Reason: The source measures endogenous and tagged association and maps CEP152 binding to the PLK4 cryptic polo-box region. The partner is a protein kinase; this supports kinase binding without assigning CEP152 kinase activity.

Proposed replacements: protein kinase binding

Summary: CEP152 directly binds the cryptic polo-box region of human PLK4.

Reason: The source combines human-cell association with purified CEP152/PLK4 fragment binding and structures. Its CEP152 peptide has a defined PLK4 interface; the fragment stoichiometry is not asserted for every full-length centrosomal complex.

Proposed replacements: protein kinase binding

Summary: CEP152 is recovered with PLK4 in the study that characterizes STIL binding.

Reason: Full Results report 16 CEP152 peptides in the U2OS PLK4 polo-box pulldown and endogenous CEP152 in myc-PLK4 immunoprecipitates (Figure 1E). The paper therefore does assay CEP152 despite its STIL-focused title. Its STIL–PB3 activation mechanism is not transferred to CEP152.

Proposed replacements: protein kinase binding

Summary: Endogenous CEP152 and CEP131 associate in human cells.

Reason: PMID:26297806 Figure 4A and Results describe reciprocal endogenous co-immunoprecipitation from HeLa lysates, with a negative control. This supports the exact association, without establishing a purified binary interface or assigning CEP131 activity to CEP152. The explicit ClinGen project instruction retains supported generic associations as non-core when the evidence does not establish a more informative molecular function.

Summary: The quantitative interactome records human CEP152 association with PLK4.

Reason: The exact IntAct source record EBI-11056636/IM-24272-432 is a positive human PLK4-bait/CEP152-prey anti-tag co-immunoprecipitation in HeLa cells. The target pair and partner class are checked; this screen alone does not prove a purified binary interface.

Proposed replacements: protein kinase binding

Summary: CEP152–PLK4 proximity is detected in the centrosome BioID study.

Reason: Exact source record EBI-11381405/IM-24512-73 links human N-terminally tagged CEP152 bait to PLK4 prey in HEK293 cells by BioID. This is proximity, not a direct binding assay. Independent human interface and biochemical studies establish the kinase-binding refinement for this same pair; the original BioID provenance is retained.

Proposed replacements: protein kinase binding

Summary: CEP152 associates with MOV10 in the human neural-cell centrosome study.

Reason: The exact source-linked IntAct records EBI-46443940, EBI-46444666 and EBI-46449862 identify O94986–Q9HCE1, human participants and neuronal precursor/neural stem-progenitor hosts. Their assay is anti-bait co-immunoprecipitation, not merely proximity labeling; all are positive records. Shared records are not counted as independent replication. The complete journal Results and Methods were not recovered. This target-level curated evidence supports association without transferring MOV10 helicase activity. The explicit ClinGen project instruction retains supported generic associations as non-core when the evidence does not establish a more informative molecular function.

Summary: The mouse-derived centriole-replication inference agrees with direct human CEP152 function.

Reason: The donor A2AUM9 is mouse Cep152 and has experimental centriole-replication support as well as inferred records. Human depletion, complementation and scaffold assays independently establish the target role, so the acceptance does not depend solely on a reciprocal electronic transfer.

Summary: CEP152 has a conserved specialized role at deuterosomes during multiciliogenesis.

Reason: The preserved Ensembl transfer uses mouse Cep152 A2AUM9. Current donor GOA links the exact process to IMP and deuterosome localization to IDA in PMID:24240477. Mouse multiciliated-cell microscopy in PMID:33627667 and Deup1-dependent compartmentalization in PMID:33658185 support this specialized context. This is retained as an ortholog-supported human function, not described as a direct human airway assay or as the universal centriole-duplication route.

Summary: CEP152 has a conserved specialized role at deuterosomes during multiciliogenesis.

Reason: The preserved Ensembl transfer uses mouse Cep152 A2AUM9. Current donor GOA links the exact process to IMP and deuterosome localization to IDA in PMID:24240477. Mouse multiciliated-cell microscopy in PMID:33627667 and Deup1-dependent compartmentalization in PMID:33658185 support this specialized context. This is retained as an ortholog-supported human function, not described as a direct human airway assay or as the universal centriole-duplication route.

Summary: CEP152 is an integral protein-complex scaffold that organizes centriole-duplication machinery.

Reason: The actual human experiments in PMID:20852615 establish distinct PLK4- and CPAP-binding regions and CEP152-dependent CPAP recruitment. Independent human CEP63–CEP152 structural/reconstitution and mutant-rescue work demonstrates an integral higher-order scaffold. Current GO:0030674 explicitly directs protein-complex scaffolds to GO:0140378. This is a source-preserving functional refinement, not a new claim of intrinsic catalysis.

Proposed replacements: protein complex scaffold activity

Summary: CEP152 is a constituent of the centrosomal CEP63–CEP152 scaffold.

Reason: The source combines human centrosomal localization with structural and reconstitution work on CEP63–CEP152 assemblies. Engineered fragments and ectopic assemblies are distinguished from endogenous centrosomal localization; the IPI source assertion is retained.

Summary: CEP152 scaffold organization supports centriole and centrosome duplication.

Reason: Mutants that disrupt CEP63–CEP152 self-assembly impair recruitment and Plk4-dependent duplication. Human-cell rescue and structural evidence support the core duplication function; the original NAS evidence code is preserved rather than upgraded.

Summary: CEP152 scaffold organization supports centriole and centrosome duplication.

Reason: Mutants that disrupt CEP63–CEP152 self-assembly impair recruitment and Plk4-dependent duplication. Human-cell rescue and structural evidence support the core duplication function; the original NAS evidence code is preserved rather than upgraded.

Summary: Human CEP152 shows supported centrosomal immunofluorescence.

Reason: The HPA source currently reports centrosome as a supported main location with antibody HPA039408. Independent human microscopy establishes that the protein acts there as a scaffold. No extra function is inferred from antibody staining.

Summary: CEP152 is detected at ciliary basal bodies in human cells.

Reason: The HPA source distinguishes supported basal-body localization in ciliated cells, including serum-starved hTERT-RPE1, from its centrosomal signal. This supports the specific location without simply equating every centriole with a basal body. It is retained as a specialized location rather than a separate core molecular activity.

Summary: Human CEP152 directly supports centriole duplication.

Reason: CEP152 depletion reduces duplication, while mapped interactions and recruitment assays place the protein within the assembly machinery. The mechanism includes CPAP recruitment and PLK4 organization, rather than only a downstream cell-cycle phenotype.

Summary: CEP152 localizes at the peripheral scaffold associated with developing centriole-assembly sites.

Reason: The source images CEP152 rings around mother and maturing daughter centrioles and PLK4 redistribution toward a SAS6-positive procentriole site. It does not place CEP152 within the cartwheel or centriole lumen. The curated procentriole-context assertion is retained together with independent human imaging of CEP152 at induced procentriole rosettes in PMID:22020124 Figure 1C; precise ring-to-procentriole geometry remains distinct from intrinsic procentriole structure.

Summary: The CEP152–PLK4 assembly is part of the procentriole replication machinery.

Reason: Direct human fragment binding and cellular assembly-site evidence support the complex annotation. The current GO definition explicitly includes CEP152:PLK4 among procentriole replication complexes. This does not imply a single stable complex containing every alternative PLK4 scaffold, or transfer fragment stoichiometry to all endogenous assemblies.

Summary: Reactome records CEP152 in a cytosolic physical-entity context.

Reason: The original Reactome:R-HSA-2574840 cytosol assertion is preserved. Its cached event narrative concerns other centrosomal or ciliary factors; it is not treated as an independent CEP152 localization assay or as evidence that CEP152 performs those partners' activities. The official human entity R-HSA-380277 explicitly maps full-length O94986 to GO:0005829. This curated compartment context is retained as non-core while the direct scaffold evidence specifies centrosomal PCM.

Summary: Reactome records CEP152 in a cytosolic physical-entity context.

Reason: The original Reactome:R-HSA-2574845 cytosol assertion is preserved. Its cached event narrative concerns other centrosomal or ciliary factors; it is not treated as an independent CEP152 localization assay or as evidence that CEP152 performs those partners' activities. The official human entity R-HSA-380277 explicitly maps full-length O94986 to GO:0005829. This curated compartment context is retained as non-core while the direct scaffold evidence specifies centrosomal PCM.

Summary: Reactome records CEP152 in a cytosolic physical-entity context.

Reason: The original Reactome:R-HSA-3000310 cytosol assertion is preserved. Its cached event narrative concerns other centrosomal or ciliary factors; it is not treated as an independent CEP152 localization assay or as evidence that CEP152 performs those partners' activities. The official human entity R-HSA-380277 explicitly maps full-length O94986 to GO:0005829. This curated compartment context is retained as non-core while the direct scaffold evidence specifies centrosomal PCM.

Summary: Reactome records CEP152 in a cytosolic physical-entity context.

Reason: The original Reactome:R-HSA-3000319 cytosol assertion is preserved. Its cached event narrative concerns other centrosomal or ciliary factors; it is not treated as an independent CEP152 localization assay or as evidence that CEP152 performs those partners' activities. The official human entity R-HSA-380277 explicitly maps full-length O94986 to GO:0005829. This curated compartment context is retained as non-core while the direct scaffold evidence specifies centrosomal PCM.

Summary: Reactome records CEP152 in a cytosolic physical-entity context.

Reason: The original Reactome:R-HSA-380272 cytosol assertion is preserved. Its cached event narrative concerns other centrosomal or ciliary factors; it is not treated as an independent CEP152 localization assay or as evidence that CEP152 performs those partners' activities. The official human entity R-HSA-380277 explicitly maps full-length O94986 to GO:0005829. This curated compartment context is retained as non-core while the direct scaffold evidence specifies centrosomal PCM.

Summary: Reactome records CEP152 in a cytosolic physical-entity context.

Reason: The original Reactome:R-HSA-380283 cytosol assertion is preserved. Its cached event narrative concerns other centrosomal or ciliary factors; it is not treated as an independent CEP152 localization assay or as evidence that CEP152 performs those partners' activities. The official human entity R-HSA-380277 explicitly maps full-length O94986 to GO:0005829. This curated compartment context is retained as non-core while the direct scaffold evidence specifies centrosomal PCM.

Summary: Reactome records CEP152 in a cytosolic physical-entity context.

Reason: The original Reactome:R-HSA-380294 cytosol assertion is preserved. Its cached event narrative concerns other centrosomal or ciliary factors; it is not treated as an independent CEP152 localization assay or as evidence that CEP152 performs those partners' activities. The official human entity R-HSA-380277 explicitly maps full-length O94986 to GO:0005829. This curated compartment context is retained as non-core while the direct scaffold evidence specifies centrosomal PCM.

Summary: Reactome records CEP152 in a cytosolic physical-entity context.

Reason: The original Reactome:R-HSA-380303 cytosol assertion is preserved. Its cached event narrative concerns other centrosomal or ciliary factors; it is not treated as an independent CEP152 localization assay or as evidence that CEP152 performs those partners' activities. The official human entity R-HSA-380277 explicitly maps full-length O94986 to GO:0005829. This curated compartment context is retained as non-core while the direct scaffold evidence specifies centrosomal PCM.

Summary: Reactome records CEP152 in a cytosolic physical-entity context.

Reason: The original Reactome:R-HSA-380311 cytosol assertion is preserved. Its cached event narrative concerns other centrosomal or ciliary factors; it is not treated as an independent CEP152 localization assay or as evidence that CEP152 performs those partners' activities. The official human entity R-HSA-380277 explicitly maps full-length O94986 to GO:0005829. This curated compartment context is retained as non-core while the direct scaffold evidence specifies centrosomal PCM.

Summary: Reactome records CEP152 in a cytosolic physical-entity context.

Reason: The original Reactome:R-HSA-380316 cytosol assertion is preserved. Its cached event narrative concerns other centrosomal or ciliary factors; it is not treated as an independent CEP152 localization assay or as evidence that CEP152 performs those partners' activities. The official human entity R-HSA-380277 explicitly maps full-length O94986 to GO:0005829. This curated compartment context is retained as non-core while the direct scaffold evidence specifies centrosomal PCM.

Summary: Reactome records CEP152 in a cytosolic physical-entity context.

Reason: The original Reactome:R-HSA-380455 cytosol assertion is preserved. Its cached event narrative concerns other centrosomal or ciliary factors; it is not treated as an independent CEP152 localization assay or as evidence that CEP152 performs those partners' activities. The official human entity R-HSA-380277 explicitly maps full-length O94986 to GO:0005829. This curated compartment context is retained as non-core while the direct scaffold evidence specifies centrosomal PCM.

Summary: Reactome records CEP152 in a cytosolic physical-entity context.

Reason: The original Reactome:R-HSA-380508 cytosol assertion is preserved. Its cached event narrative concerns other centrosomal or ciliary factors; it is not treated as an independent CEP152 localization assay or as evidence that CEP152 performs those partners' activities. The official human entity R-HSA-380277 explicitly maps full-length O94986 to GO:0005829. This curated compartment context is retained as non-core while the direct scaffold evidence specifies centrosomal PCM.

Summary: Reactome records CEP152 in a cytosolic physical-entity context.

Reason: The original Reactome:R-HSA-5617816 cytosol assertion is preserved. Its cached event narrative concerns other centrosomal or ciliary factors; it is not treated as an independent CEP152 localization assay or as evidence that CEP152 performs those partners' activities. The official human entity R-HSA-380277 explicitly maps full-length O94986 to GO:0005829. This curated compartment context is retained as non-core while the direct scaffold evidence specifies centrosomal PCM.

Summary: Reactome records CEP152 in a cytosolic physical-entity context.

Reason: The original Reactome:R-HSA-5626220 cytosol assertion is preserved. Its cached event narrative concerns other centrosomal or ciliary factors; it is not treated as an independent CEP152 localization assay or as evidence that CEP152 performs those partners' activities. The official human entity R-HSA-380277 explicitly maps full-length O94986 to GO:0005829. This curated compartment context is retained as non-core while the direct scaffold evidence specifies centrosomal PCM.

Summary: Reactome records CEP152 in a cytosolic physical-entity context.

Reason: The original Reactome:R-HSA-5626223 cytosol assertion is preserved. Its cached event narrative concerns other centrosomal or ciliary factors; it is not treated as an independent CEP152 localization assay or as evidence that CEP152 performs those partners' activities. The official human entity R-HSA-380277 explicitly maps full-length O94986 to GO:0005829. This curated compartment context is retained as non-core while the direct scaffold evidence specifies centrosomal PCM.

Summary: Reactome records CEP152 in a cytosolic physical-entity context.

Reason: The original Reactome:R-HSA-5626227 cytosol assertion is preserved. Its cached event narrative concerns other centrosomal or ciliary factors; it is not treated as an independent CEP152 localization assay or as evidence that CEP152 performs those partners' activities. The official human entity R-HSA-380277 explicitly maps full-length O94986 to GO:0005829. This curated compartment context is retained as non-core while the direct scaffold evidence specifies centrosomal PCM.

Summary: Reactome records CEP152 in a cytosolic physical-entity context.

Reason: The original Reactome:R-HSA-5626228 cytosol assertion is preserved. Its cached event narrative concerns other centrosomal or ciliary factors; it is not treated as an independent CEP152 localization assay or as evidence that CEP152 performs those partners' activities. The official human entity R-HSA-380277 explicitly maps full-length O94986 to GO:0005829. This curated compartment context is retained as non-core while the direct scaffold evidence specifies centrosomal PCM.

Summary: Reactome records CEP152 in a cytosolic physical-entity context.

Reason: The original Reactome:R-HSA-5626681 cytosol assertion is preserved. Its cached event narrative concerns other centrosomal or ciliary factors; it is not treated as an independent CEP152 localization assay or as evidence that CEP152 performs those partners' activities. The official human entity R-HSA-380277 explicitly maps full-length O94986 to GO:0005829. This curated compartment context is retained as non-core while the direct scaffold evidence specifies centrosomal PCM.

Summary: Reactome records CEP152 in a cytosolic physical-entity context.

Reason: The original Reactome:R-HSA-5626699 cytosol assertion is preserved. Its cached event narrative concerns other centrosomal or ciliary factors; it is not treated as an independent CEP152 localization assay or as evidence that CEP152 performs those partners' activities. The official human entity R-HSA-380277 explicitly maps full-length O94986 to GO:0005829. This curated compartment context is retained as non-core while the direct scaffold evidence specifies centrosomal PCM.

Summary: Reactome records CEP152 in a cytosolic physical-entity context.

Reason: The original Reactome:R-HSA-5638009 cytosol assertion is preserved. Its cached event narrative concerns other centrosomal or ciliary factors; it is not treated as an independent CEP152 localization assay or as evidence that CEP152 performs those partners' activities. The official human entity R-HSA-380277 explicitly maps full-length O94986 to GO:0005829. This curated compartment context is retained as non-core while the direct scaffold evidence specifies centrosomal PCM.

Summary: Reactome records CEP152 in a cytosolic physical-entity context.

Reason: The original Reactome:R-HSA-8853405 cytosol assertion is preserved. Its cached event narrative concerns other centrosomal or ciliary factors; it is not treated as an independent CEP152 localization assay or as evidence that CEP152 performs those partners' activities. The official human entity R-HSA-380277 explicitly maps full-length O94986 to GO:0005829. This curated compartment context is retained as non-core while the direct scaffold evidence specifies centrosomal PCM.

Summary: Reactome records CEP152 in a cytosolic physical-entity context.

Reason: The original Reactome:R-HSA-8853419 cytosol assertion is preserved. Its cached event narrative concerns other centrosomal or ciliary factors; it is not treated as an independent CEP152 localization assay or as evidence that CEP152 performs those partners' activities. The official human entity R-HSA-380277 explicitly maps full-length O94986 to GO:0005829. This curated compartment context is retained as non-core while the direct scaffold evidence specifies centrosomal PCM.

Summary: Human CEP152 co-precipitates with CCDC66.

Reason: PMID:35849559 Figure 2E tests FLAG-miniTurbo–CCDC66 with myc-BirA*–CEP152 in HEK293T cells using FLAG co-immunoprecipitation and tag controls. The fusion names do not make this particular assay BioID. The exact association is supported without claiming a purified interface or transferring CCDC66 microtubule activity. The explicit ClinGen project instruction retains supported generic associations as non-core when the evidence does not establish a more informative molecular function.

Summary: CEP152 is localized to mitotic centrosomes in human cells.

Reason: The source includes CEP152 immunofluorescence at mitotic U2OS centrosomes. The CCDC66 perturbation and microtubule-function conclusions are not assigned to CEP152 simply because it is used as a centrosomal partner or marker.

Summary: CEP152 localizes at mature, duplication-competent centriole-associated PCM.

Reason: PMID:32060285 Figure 2e/f and Results directly compare CEP152 at centrioles in control versus CEP44-depleted human cells. This supports its location; CEP44-dependent wall integrity and conversion are not treated as intrinsic CEP152 structural-wall activities.

Summary: Human CEP152 is detected at centriole/procentriole assemblies.

Reason: The full source Figure 1C reports CEP152 immunofluorescence at STIL-induced procentriole rosettes in U2OS cells. This is actual target localization despite the STIL-focused title. Its separate negative STIL–CEP152 co-IP result does not negate the location.

Summary: CEP152 occupies pericentriolar material around centrioles.

Reason: The source uses CEP152 immunostaining as the external PCM ring relative to lumen-localized MDM1 in human RPE1 cells. Independent human immunogold and super-resolution studies support this core structural location. MDM1 microtubule-binding activity is not transferred.

Summary: CEP152 is associated with the proximal peripheral region of centrioles.

Reason: The source distinguishes the CEP152 PCM ring from the MDM1-filled lumen. The broad centriolar location is valid without making CEP152 an intrinsic centriole-wall or lumen component.

Summary: The ortholog-transfer assertion is concordant with direct human centriole-replication evidence.

Reason: Mouse A2AUM9 is the preserved donor in the original GOA. The target itself has experimental human scaffold and duplication data, so this remains a valid inherited functional assertion; it is not rejected merely because additional donor annotations point back to human CEP152.

Summary: The specialized deuterosome role is supported by the experimentally studied frog ortholog.

Reason: The actual donor Q498G2 is Xenopus laevis Cep152, not mouse or rat. Donor GOA links these exact terms to PMID:24075808. Full Results Figures 3–4 and Methods identify tagged frog Cep152 at deuterosomes and nascent centrioles; overexpression and the first-306-residue dominant-negative construct alter amplification, with PLK4 coexpression rescue. This supports the conserved scaffold context while retaining the source as a human ortholog inference rather than a direct human experiment.

Summary: The specialized deuterosome role is supported by the experimentally studied frog ortholog.

Reason: The actual donor Q498G2 is Xenopus laevis Cep152, not mouse or rat. Donor GOA links these exact terms to PMID:24075808. Full Results Figures 3–4 and Methods identify tagged frog Cep152 at deuterosomes and nascent centrioles; overexpression and the first-306-residue dominant-negative construct alter amplification, with PLK4 coexpression rescue. This supports the conserved scaffold context while retaining the source as a human ortholog inference rather than a direct human experiment.

Summary: The proteomics-derived centrosome annotation agrees with established human CEP152 localization.

Reason: The source is a genuine human centrosome purification/proteomics study. Its exact supplementary target row was not separately re-extracted during this audit, so it is not claimed as a newly verified target assay. The curated source is retained and direct human immunofluorescence, immunogold and structural-localization evidence independently support the location.

Summary: The CEP152–CPAP interaction contributes to the centriole-duplication scaffold.

Reason: The source directly tests human CEP152 binding to CPAP and CEP152-dependent centrosomal recruitment. Together with separate PLK4 binding and later CEP63–CEP152 structural work, this establishes a scaffold role beyond a generic interaction. Current GO directs integral complex scaffolds to GO:0140378; CPAP tubulin-related activity is not transferred to CEP152.

Proposed replacements: protein complex scaffold activity

Summary: Human CEP152 associates with CINP.

Reason: The full paper and Supplementary Figure 8 test GFP- or FLAG-tagged CINP co-immunoprecipitation with endogenous CEP152 in HEK293T cells. Supplementary Methods additionally describe a human ORF-library yeast two-hybrid screen using CEP152 residues 1–152, with three CINP hits. These assays support the association, not an intrinsic checkpoint-enzyme activity or a newly demonstrated purified full-length interface. The explicit ClinGen project instruction retains supported generic associations as non-core when the evidence does not establish a more informative molecular function.

Summary: Human CEP152 localizes to centrosomes.

Reason: PMID:21131973 Figure 2a shows GFP-tagged wild-type human CEP152 at pericentrin-positive centrosomes in HEK293T cells; the supplement documents the human full-length clone. Patient-cell genome-instability phenotypes are distinct from this directly observed localization.

Summary: PLK4 binding is an established component of CEP152 scaffold function.

Reason: Human binding and recruitment experiments directly support association with the protein kinase PLK4 through the CEP152 N-terminal region. This is kinase binding, not intrinsic CEP152 kinase catalysis or an assertion that CEP152 alone activates PLK4.

Summary: PLK4 binding is an established component of CEP152 scaffold function.

Reason: Human binding and recruitment experiments directly support association with the protein kinase PLK4 through the CEP152 N-terminal region. This is kinase binding, not intrinsic CEP152 kinase catalysis or an assertion that CEP152 alone activates PLK4.

Summary: Human CEP152 supports centrosome duplication.

Reason: The source tests CEP152 knockdown and overexpression in human U2OS cells, including aphidicolin-induced centriole reduplication, and maps partner recruitment. These are direct functional experiments; the detailed fly Asl microtubule-organizing phenotypes are not transferred wholesale.

Summary: CEP152 regulates spindle assembly through its centrosomal inhibitory complex and APC/C recruitment.

Reason: This corrects the inherited reviewer-authored NEW proposal from direct spindle assembly to regulation of mitotic spindle assembly; the original proposed object is preserved in audit provenance. PMID:34878135 Figures 3–5 show APC/C association despite mutated substrate-recognition motifs, CEP152-dependent centrosomal APC/C recruitment while centrioles remain, and increased CEP57–pericentrin association/recruitment after CEP152 depletion. Thus CEP152 performs regulatory work beyond being a substrate. DBK mutant persistence delays microtubule nucleation and bipolar spindle formation. The study does not demonstrate a purified direct APC/C interface; its Discussion explicitly allows ubiquitylation-dependent relocation without obligatory degradation. GO:1901673 captures this regulation more precisely than calling CEP152 a spindle-building component.