Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Asterless is a scaffold for the onset of centriole assembly.
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CEP152 is a molecular platform with separated PLK4- and CPAP-binding regions and is required for centrosome duplication.
"Here we show that the centriolar protein Asterless (Asl; human orthologue CEP152) provides a conserved molecular platform, the amino terminus of which interacts with the cryptic Polo box of Plk4 whereas the carboxy terminus interacts with the centriolar protein Sas-4 (CPAP in humans)."
Cep152 acts as a scaffold for recruitment of Plk4 and CPAP to the centrosome.
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CEP152 recruits PLK4 and CPAP to the centrosome for faithful duplication.
"Our results suggest that Cep152 recruits Plk4 and CPAP to the centrosome to ensure a faithful centrosome duplication process."
CEP152 is a genome maintenance protein disrupted in Seckel syndrome.
Novel asymmetrically localizing components of human centrosomes identified by complementary proteomics methods.
The human microcephaly protein STIL interacts with CPAP and is required for procentriole formation.
Molecular basis for unidirectional scaffold switching of human Plk4 in centriole biogenesis.
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PLK4 relocates from a CEP192 ring to a newly assembled CEP152 ring during centriole biogenesis.
"We show that Plk4 relocalizes from the inner Cep192 ring to the outer Cep152 ring as newly recruited Cep152 assembles around the Cep192-encircled daughter centriole."
STIL binding to Polo-box 3 of PLK4 regulates centriole duplication.
Centriolar satellites assemble centrosomal microcephaly proteins to recruit CDK2 and promote centriole duplication.
MDM1 is a microtubule-binding protein that negatively regulates centriole duplication.
A human interactome in three quantitative dimensions organized by stoichiometries and abundances.
A Dynamic Protein Interaction Landscape of the Human Centrosome-Cilium Interface.
Molecular architecture of a cylindrical self-assembly at human centrosomes.
CEP44 ensures the formation of bona fide centriole wall, a requirement for the centriole-to-centrosome conversion.
Spatial centrosome proteome of human neural cells uncovers disease-relevant heterogeneity.
The ciliopathy protein CCDC66 controls mitotic progression and cytokinesis by promoting microtubule nucleation and organization.
AJUBA facilitates AURKA autophosphorylation
AJUBA binds centrosome-associated AURKA
AURKA phosphorylates PLK1
BORA binds PLK1 and AURKA
Plk1-mediated phosphorylation of Nlp
Recruitment of additional gamma tubulin/ gamma TuRC to the centrosome
Loss of C-Nap-1 from centrosomes
Dissociation of Phospho-Nlp from the centrosome
Recruitment of Plk1 to centrosomes
Association of NuMA with microtubules
Recruitment of CDK11p58 to the centrosomes
Translocation of NuMA to the centrosomes
RAB3IP stimulates nucleotide exchange on RAB8A
C2CD3 binds the mother centriole
C2CD3 and OFD1 recruit 5 distal appendage proteins to the centriole
CP110 and CEP97 dissociate from the centriole
The distal appendage proteins recruit TTBK2
Recruitment of transition zone proteins
MARK4 binds ODF2 in the centriole
CEP164 recruits RAB3IP-carrying Golgi-derived vesicles to the basal body
TPX2 binds AURKA at centrosomes
TPX2 promotes AURKA autophosphorylation
Mutations in centrosomal protein CEP152 in primary microcephaly families linked to MCPH4.
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A truncating disease allele prevents CEP152 localization to centrosomes in transfected cells.
"The third affected child was compound heterozygous for the missense mutation plus a second, premature-termination mutation truncating a third of the protein and preventing its localization to centrosomes in transfected cells."
Cep152 interacts with Plk4 and is required for centriole duplication.
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CEP152 depletion blocks normal and PLK4-induced centriole formation.
"Depletion of Cep152 prevents both normal centriole duplication and Plk4-induced centriole amplification and results in a failure to localize Sas6 to the centriole, an early step in duplication."
Fibrogranular materials function as organizers to ensure the fidelity of multiciliary assembly.
Biophysical and biochemical properties of Deup1 self-assemblies: a potential driver for deuterosome formation during multiciliogenesis.
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DEUP1 self-assemblies recruit CEP152 and PLK4 in multiciliated-cell models.
"Using an optogenetic approach, we demonstrated that self-assembly and the C-terminal half of Deup1 were sufficient to spatially compartmentalize centrosomal protein 152 (Cep152) and polo like kinase 4 (Plk4), master components for centriole biogenesis, in the cytoplasm."
The APC/C targets the Cep152-Cep63 complex at the centrosome to regulate mitotic spindle assembly.
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APC/C-dependent CEP152 turnover is required for proper mitotic spindle assembly.
"This negative feedback loop controlling APC/C localization is required for proper assembly of the mitotic spindle."
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Stabilizing APC/C-resistant CEP152 impairs microtubule nucleation and chromosome segregation.
"Stabilization of a Cep152 mutant that cannot be targeted by the APC/C results in reduced microtubule nucleation and increased chromosome mis-segregation."
Architectural basis for cylindrical self-assembly governing Plk4-mediated centriole duplication in human cells.
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CEP63-CEP152 heterotetramer assembly organizes CEP152 and PLK4 for centriole duplication.
"Mutants defective in Cep63•Cep152 heterotetramer formation displayed crippled pericentriolar Cep152 organization, polo-like kinase 4 (Plk4) relocalization to the procentriole assembly site, and Plk4-mediated centriole duplication."
Manual deep research synthesis for human CEP152