Affinage

CCDC77

Coiled-coil domain-containing protein 77 · UniProt Q9BR77

Length
488 aa
Mass
57.5 kDa
Annotated
2026-06-09
5 papers in source corpus 2 papers cited in narrative 2 extracted findings
Cross-family judge faithfulness: 3/3 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

CCDC77 is a structural component of the centriole A-C linker, a connector positioned between adjacent microtubule triplets in the proximal region of the organelle (PMID:40707486). Within this structure CCDC77 assembles into a complex with WDR67 and MIIP, and its depletion disrupts microtubule triplet cohesion, causing breakage at the proximal end of the centriole; combined removal of the A-C linker and the inner scaffold demonstrates their joint requirement for maintaining overall centriole architecture (PMID:40707486). Beyond its structural role, the A-C linker including CCDC77 contributes to centriole duplication through regulation of the torus (PMID:40707486). Beyond these findings, no further mechanistic detail for CCDC77 has been characterized in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 2 steps
  1. 2024 Medium

    Established where CCDC77 sits in centriole ultrastructure and what it binds, addressing whether this uncharacterized coiled-coil protein has a defined structural role at the centriole.

    Evidence Ultrastructure expansion microscopy, protein depletion, and complex-formation analysis (preprint)

    PMID:bio_10.1101_2024.10.04.616628

    Open questions at the time
    • Preprint version, not yet peer reviewed
    • Stoichiometry and direct binding interfaces within the WDR67/MIIP complex not resolved
    • Molecular basis of torus regulation in duplication unexplained
  2. 2025 High

    Confirmed CCDC77 as an A-C linker protein between microtubule triplets that, in complex with WDR67 and MIIP, is required for triplet cohesion, centriole integrity, and duplication via the torus, establishing its function in maintaining centriole architecture.

    Evidence U-ExM, knockdown/knockout depletion with phenotyping, co-localization and complex formation analysis in cultured cells

    PMID:40707486

    Open questions at the time
    • Mechanism by which the A-C linker regulates the torus during duplication unresolved
    • No structure of the CCDC77–WDR67–MIIP complex
    • Direct versus indirect contributions of CCDC77 to cohesion not separated from other A-C linker components

Open questions

Synthesis pass · forward-looking unresolved questions
  • How CCDC77 mechanistically couples A-C linker integrity to torus-dependent centriole duplication remains unknown.
  • No biochemical reconstitution of the complex
  • No structural model of the A-C linker
  • Recruitment hierarchy among CCDC77, WDR67, and MIIP undefined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0005198 structural molecule activity 1
Localization
GO:0005815 microtubule organizing center 1
Pathway
R-HSA-1852241 Organelle biogenesis and maintenance 1
Partners
MIIPWDR67
Complex memberships
CCDC77-WDR67-MIIP A-C linker complex

Evidence

Reading pass · 2 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2025 CCDC77 localizes to the A-C linker structure of centrioles, positioned between microtubule triplets in the proximal region, where it forms a complex with WDR67 and MIIP. Depletion of CCDC77 (along with other A-C linker components) disrupts microtubule triplet cohesion, causing breakage at the proximal end of the centriole. Co-removal of the A-C linker and the inner scaffold reveals their joint role in maintaining centriole architecture. Additionally, the A-C linker (including CCDC77) plays an unexpected role in centriole duplication through torus regulation. Ultrastructure expansion microscopy (U-ExM), protein depletion (knockdown/knockout), co-localization and complex formation analysis Nature communications High 40707486
2024 CCDC77 localizes to the A-C linker of centrioles between microtubule triplets, forming a complex with WDR67 and MIIP; depletion of A-C linker components disrupts triplet cohesion and centriole duplication via torus regulation (preprint version of the same study). Ultrastructure expansion microscopy, protein depletion, complex formation analysis bioRxivpreprint Medium bio_10.1101_2024.10.04.616628

Source papers

Stage 0 corpus · 5 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2014 A 1.5Mb terminal deletion of 12p associated with autism spectrum disorder. Gene 20 24613754
2024 Integration of Multi-Omics Data for the Classification of Glioma Types and Identification of Novel Biomarkers. Bioinformatics and biology insights 11 38812741
2025 The A-C linker controls centriole structural integrity and duplication. Nature communications 10 40707486
2026 Identification of novel candidate neural genes for diet-induced obesity in outbred heterogeneous stock rats. Research square 0 42239780
2025 Saliva as a potential and non-invasive approach to identify upregulated genes associated with comorbidities of T1DM: a brief report. European journal of medical research 0 41074104

Missed literature

Know a paper Affinage missed for CCDC77? Flag it for the maintainers and the community.

No submissions yet.