Cep164, a novel centriole appendage protein required for primary cilium formation.

Centriole distal appendages promote membrane docking, leading to cilia initiation.

Cep164 triggers ciliogenesis by recruiting Tau tubulin kinase 2 to the mother centriole.

Binding to Cep164, but not EB1, is essential for centriolar localization of TTBK2 and its function in ciliogenesis.

Molecular mechanisms underlying the role of the centriolar CEP164-TTBK2 complex in ciliopathies.

Cep164 mediates vesicular docking to the mother centriole during early steps of ciliogenesis.

Phosphatidylinositol phosphate kinase PIPKIγ and phosphatase INPP5E coordinate initiation of ciliogenesis.

Exome capture reveals ZNF423 and CEP164 mutations, linking renal ciliopathies to DNA damage response signaling.

Cep164 is a mediator protein required for the maintenance of genomic stability through modulation of MDC1, RPA, and CHK1.

CEP164-null cells generated by genome editing show a ciliation defect with intact DNA repair capacity.

Comparison of tear protein levels in breast cancer patients and healthy controls using a de novo proteomic approach.

Super-resolution architecture of mammalian centriole distal appendages reveals distinct blade and matrix functional components.

Deep research report on CEP164 (falcon)

Intrinsic heterogeneity of primary cilia revealed through spatial proteomics.

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

Electronic Gene Ontology annotations created by ARBA machine learning models

Combined Automated Annotation using Multiple IEA Methods

Novel asymmetrically localizing components of human centrosomes identified by complementary proteomics methods.

CCDC41 is required for ciliary vesicle docking to the mother centriole.

The CP110-interacting proteins Talpid3 and Cep290 play overlapping and distinct roles in cilia assembly.

MDM1 is a microtubule-binding protein that negatively regulates centriole duplication.

A Conserved Role for Girdin in Basal Body Positioning and Ciliogenesis.

A reference map of the human binary protein interactome.

Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.

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 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

CEP164 bounded source evidence

CEP164 primary-source scope and access ledger

Characterization of membrane structures regulating primary ciliogenesis by quantitative isotropic ultrastructure imaging.