| 2010 |
CEP152 interacts with the cryptic Polo-box (CPB) of PLK4 via its N-terminal domain (first 217 residues), and this interaction is required for PLK4 recruitment to centrosomes and for PLK4-induced centriole overduplication. |
Co-immunoprecipitation, overexpression of truncated CEP152(1-217) to mislocalize PLK4, siRNA knockdown with centriole duplication readout |
The Journal of cell biology |
High |
21059844 21059850
|
| 2010 |
CEP152 is required for recruitment of CPAP to the centrosome; depletion of CEP152 causes loss of CPAP, monopolar mitotic spindles, and failure of centriole duplication. |
siRNA knockdown, immunofluorescence for CPAP and centriole markers, spindle formation assay |
The Journal of cell biology |
Medium |
21059844
|
| 2010 |
CEP152 can be phosphorylated by PLK4 in vitro, indicating CEP152 is a PLK4 substrate. |
In vitro kinase assay with recombinant PLK4 and CEP152 |
The Journal of cell biology |
Medium |
21059850
|
| 2010 |
CEP152 loss-of-function leads to accumulation of genomic defects through replicative stress, enhanced ATM signaling activation, and increased H2AX phosphorylation, identifying CEP152 as a genome maintenance/DNA damage response regulator. |
Homozygosity mapping and exome sequencing to identify CEP152 mutations in Seckel syndrome; functional assays measuring ATM signaling and H2AX phosphorylation in patient-derived cells |
Nature genetics |
Medium |
21131973
|
| 2010 |
A CEP152 truncation mutation that removes one-third of the protein prevents its localization to centrosomes, demonstrating that the C-terminal region is required for centrosomal targeting. |
Transfection of truncated CEP152 construct in cells, immunofluorescence microscopy |
American journal of human genetics |
Medium |
20598275
|
| 2008 |
CEP152 (vertebrate ortholog of Drosophila Asterless/Asl) is essential for daughter centriole formation; depletion eliminates multiple centriolar markers while only mildly affecting pericentriolar material (PCM) function, placing CEP152 early in centriole duplication. CEP152/Asl localizes closely associated with the centriole wall but is not part of the centriole structure itself. |
Loss-of-function allele characterization in Drosophila (mecD asl allele), morpholino knockdown in zebrafish, immunolocalization of centriole markers and PCM components |
Genetics |
Medium |
18854586
|
| 2013 |
CEP192 and CEP152 cooperate to recruit PLK4 to mammalian centrioles: CEP192 is required for centrosomal recruitment of CEP152 (placing CEP192 upstream), and double-depletion of both proteins completely abolishes PLK4 binding and centriole duplication. PLK4 binding regions of CEP192 and CEP152 (residues 190–240 and 1–46, respectively) are rich in negatively charged amino acids, suggesting electrostatic interactions with PLK4's positively charged polo-box domain. |
Sequential siRNA double-depletion, Co-IP, domain-deletion mapping, super-resolution microscopy |
Journal of cell science |
High |
23641073 24277814
|
| 2013 |
CEP192 and CEP152 serve as two distinct hierarchical scaffolds that recruit PLK4 to distinct subcentrosomal regions in a temporally regulated manner; CEP192 and CEP152 competitively interact with the cryptic polo-box of PLK4 through homologous N-terminal sequences containing acidic-α-helix and N/Q-rich motifs. Expression of either N-terminal fragment alone is sufficient to delocalize PLK4 from centrosomes. |
Biochemical competition assays, Co-IP with truncated constructs, live-cell imaging, loss-of-function by depletion with centriole duplication readout |
Proceedings of the National Academy of Sciences of the United States of America |
High |
23641073 24277814
|
| 2013 |
CEP57, CEP63, and CEP152 form a ring-like complex localizing around the proximal end of centrioles, as revealed by selective chemical crosslinking and super-resolution microscopy. CEP152 and PLK4 reside in two separable structures at the centrosome, suggesting PLK4 contacts CEP152 only transiently. |
Selective chemical crosslinking (SNAP-tag-based), super-resolution (STED) microscopy, pulldown assays |
Current biology : CB |
High |
23333316
|
| 2018 |
In mouse oocytes (acentriolar MTOCs), CEP152 localizes to MTOCs at the germinal vesicle stage and is excluded from MTOCs after germinal vesicle breakdown; this exclusion is regulated by CDK1 activity and is involved in MTOC fragmentation during meiotic spindle formation. |
Live-cell imaging, immunofluorescence of staged oocytes, siRNA depletion with CDK1 inhibitor treatment and MTOC/spindle morphology readouts |
FASEB journal |
Medium |
28970258
|
| 2020 |
CEP63 and CEP152 cooperatively form a heterotetrameric complex that undergoes liquid-liquid phase separation (LLPS) to generate higher-order self-assemblies at centrosomes. Two hydrophobic motifs, one each from CEP63 and CEP152, are required for phase-separating condensates and high-molecular-weight assembly. LLPS disruptor 1,6-hexanediol diminishes endogenous CEP63 and CEP152 centrosome localization. |
In vitro reconstitution of purified CEP63•CEP152 complex, FRAP, hexanediol treatment, mutagenesis of hydrophobic motifs, correlative light-electron microscopy (CLEM) |
Cell cycle (Georgetown, Tex.) |
High |
33208041
|
| 2022 |
The APC/C ubiquitin ligase localizes to centrosomes specifically during mitosis, requires CEP152 for this centrosomal recruitment, ubiquitylates CEP152 as a substrate, and thereby releases CEP57 from the inhibitory CEP152-CEP57-CEP63 complex, enabling CEP57 to interact with pericentrin and promote microtubule nucleation. |
Co-IP identifying CEP152 as APC/C interaction partner and substrate; functional assays showing APC/C-mediated ubiquitylation of CEP152; immunofluorescence of CEP57-pericentrin interaction upon CEP152 degradation |
Journal of cell science |
Medium |
34878135
|
| 2023 |
At nanoscale resolution, CEP152 (the major PLK4 receptor) develops a complex, non-nine-fold-symmetric pattern at mature centrioles, distinct from CEP57, CEP63, CEP44, and CEP192 which retain ninefold symmetry. This molecular arrangement of CEP152 creates flexibility for PLK4 and procentriole placement, enabling procentrioles to form at variable positions relative to mother centriole microtubule triplets. |
Expansion microscopy and super-resolution fluorescence microscopy (U-ExM), quantitative positional mapping of CEP152, PLK4, and other centriole components |
The Journal of cell biology |
Medium |
37707473
|
| 2025 |
Binding of the N-terminal part of CEP152 to PLK4 increases PLK4 phosphorylation and kinase activation, likely by stabilizing PLK4 dimer formation to promote autophosphorylation. CEP152 degradation disrupts PLK4 localization at the proximal centriole end and reduces phosphorylated PLK4 levels there. |
Auxin-inducible degron (AID) system for rapid CEP152 degradation in engineered cell lines; kinase activity assays; immunofluorescence for phospho-PLK4 |
Molecular biology of the cell |
Medium |
40372713
|
| 2025 |
PLK4 homodimerization via its CPB is required to maintain CEP152 at S-phase centrosomes; a cancer-associated PLK4 truncation mutation disrupting the CPB prevents PLK4 homodimerization, abrogates CEP152 and CEP192 interaction, reduces centrosomal CEP152 and pericentrin, and causes unfocused spindles and reduced cell viability. |
Cancer variant characterization, Co-IP of PLK4 mutants with CEP152/CEP192, immunofluorescence, cell viability assay |
Journal of molecular biology |
Medium |
40222413
|
| 2025 |
CEP152, CEP63, and PCNT form aggregates (cartwheel seeds, CSs) that act as seeds for cartwheel assembly independently of centrioles; these CSs form in interphase as nanoscale concentric rings of CEP152 and CEP63, recruit ALMS1 upon mitotic entry, and disassemble under ALMS1 control. ALMS1 depletion abolishes CS formation and eliminates centrioles. |
Super-resolution microscopy (U-ExM, SIM), TurboID proximity labeling, Co-IP, ALMS1 depletion/rescue experiments, immunofluorescence of centriole markers |
bioRxivpreprint |
Medium |
40667363
|
| 2022 |
CEP152 is expressed in the centrosome of neuronal progenitors in the ventricular zone during embryonic brain development (E14) and also localizes to excitatory postsynaptic sites (co-localizing with PSD95 and synaptophysin) in differentiated hippocampal neurons, suggesting a role beyond centriole duplication in differentiated neurons. |
Immunohistochemistry, subcellular fractionation (postsynaptic density fraction), immunofluorescence co-localization in primary cultured hippocampal neurons |
Developmental neuroscience |
Low |
35259752
|
| 2026 |
Distinct CEP152 variant classes disrupt centriole function by different mechanisms: the p.K897* variant prevents centrosomal localization of CEP152, p.W105* leads to protein degradation, and p.Q32P retains centrosomal targeting but specifically disrupts binding to PLK4, causing centrosome structural abnormalities and mitotic errors in knock-in mouse brains. |
In vitro localization assays of mutant CEP152 constructs, Co-IP for PLK4 binding, knock-in mouse models with cortical phenotype analysis, electron microscopy of centriole structure, immunofluorescence for mitotic errors |
EMBO molecular medicine |
High |
42086905
|
| 2026 |
NuSAP localizes to centrioles and directly interacts with CEP57; NuSAP depletion disrupts centriole tubulin architecture and prevents recruitment of the CEP57-CEP63-CEP152 torus complex to the proximal end of procentrioles, establishing a two-step model where NuSAP-dependent tubulin stabilization is required for initial CEP57 loading upstream of CEP152 torus assembly. |
Super-resolution microscopy, TurboID-based proximity proteomics, Co-IP of NuSAP with CEP57, siRNA depletion with immunofluorescence readout |
Advanced science |
Medium |
41616107
|