ArticleScience advances2026
CCDC32 collaborates with the membrane to assemble the AP-2 clathrin adaptor complex.
Article in Science advances, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
3 citing papers in PubMed.
- Structural mechanisms of cargo adaptors in membrane trafficking.Current opinion in cell biology · 2026Review
- AP2: an indispensable host factor in virus infection.Journal of virology · 2026Review
- Regulation of AP1 adaptor assembly by the bi-handed chaperone MEA1.Nature communications · 2026Article
Corrections and comments
- Update of
Authors and funding
11 authors.
Funding
Abstract
Assembly of adaptor protein complex 2 (AP-2), the primary cargo adaptor in clathrin-mediated endocytosis, is regulated by the chaperones alpha- and gamma-adaptin binding protein (AAGAB) and coiled-coil domain-containing protein 32 (CCDC32), whose deletion causes loss of all AP-2 subunits in vivo. Here, we describe the molecular mechanism of CCDC32-mediated AP-2 assembly. CCDC32 interacts with the appendage domain of the AP-2 α subunit with high affinity, using the same binding site as canonical endocytic regulators in addition to a previously unidentified, yet highly conserved pocket on α. CCDC32 contains cargo sorting motifs normally found in transmembrane cargo and binds to AP-2 heterodimers using canonical cargo-binding sites. In addition, two amphipathic helices in CCDC32 bind to the α/σ2 heterodimer. Unexpectedly, in solution, CCDC32 prevents complex assembly and actively disassembles AP-2 tetramers. Inhibition requires the amphipathic helices of CCDC32, which also mediate binding to phosphatidylinositol 4,5-bisphosphate (PIP
Indexed as
Identifiers
What Socratic holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.