ArticleCell2010
A large-scale conformational change couples membrane recruitment to cargo binding in the AP2 clathrin adaptor complex.
Article in Cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 221 papers.
What it found
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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
221 citing papers in PubMed, 393 citations in OpenAlex.
- Phosphoglycerate kinase 1 cooperates with the AP2 complex to promote endocytosis.EMBO reports · 2026Article
- Interview With Barbara Pearse and the Clathrin Family Tree.Traffic (Copenhagen, Denmark) · 2026Article
- The multifaceted significance of phosphoinositides in endocytic trafficking.FEBS letters · 2026Review
- CCDC32 collaborates with the membrane to assemble the AP-2 clathrin adaptor complex.Science advances · 2026Article
- NECAP antagonizes light-induced Rhodopsin-1 internalization to promote photoreceptor homeostasis.bioRxiv : the preprint server for biology · 2026Article
- Zinc-induced exposure of an LxL motif drives clathrin-mediated endocytosis of the zinc transceptor ZIP4.The Journal of biological chemistry · 2026Article
- Architecture of clathrin-independent AP3:ARF1-coated carriers.Science advances · 2026Article
- Clathrin-mediated endocytosis of ERECTA family receptors is essential for proper stomatal development inProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Oncometabolite 5-IPNature chemical biology · 2026Article
- Structural basis for the dynamic conformations of AP-4 and its association with ARF1.Nature communications · 2026Article
- Regulation of AP1 adaptor assembly by the bi-handed chaperone MEA1.Nature communications · 2026Article
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- Measuring and locating the changes in protein structure using MELO.Nature communications · 2026Article
- Article
- VapA/Scs2 sustains polarized growth inMicrobial cell (Graz, Austria) · 2026Article
- ARCN1 suppresses innate immune responses against respiratory syncytial virus by promoting STUB1-mediated IKKε degradation.PLoS pathogens · 2025Article
- Modeling AP2M1 developmental and epileptic encephalopathy in Drosophila.Disease models & mechanisms · 2025Article
- A combined biochemical and computational approach provides evidence for membrane remodelling by the structural scaffold of the endocytic TPLATE complex.Nature plants · 2025Article
- Canonical tyrosine-based motifs are required for constitutive endocytosis and polarity of IRT1 and contribute to metal uptake.The Plant journal : for cell and molecular biology · 2025Article
- Bi-handed assembly chaperones regulate protein complex assembly through an intramolecular handover mechanism.Science advances · 2025Article
161 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
The AP2 adaptor complex (alpha, beta2, sigma2, and mu2 subunits) crosslinks the endocytic clathrin scaffold to PtdIns4,5P(2)-containing membranes and transmembrane protein cargo. In the "locked" cytosolic form, AP2's binding sites for the two endocytic motifs, YxxPhi on the C-terminal domain of mu2 (C-mu2) and [ED]xxxL[LI] on sigma2, are blocked by parts of beta2. Using protein crystallography, we show that AP2 undergoes a large conformational change in which C-mu2 relocates to an orthogonal face of the complex, simultaneously unblocking both cargo-binding sites; the previously unstructured mu2 linker becomes helical and binds back onto the complex. This structural rearrangement results in AP2's four PtdIns4,5P(2)- and two endocytic motif-binding sites becoming coplanar, facilitating their simultaneous interaction with PtdIns4,5P(2)/cargo-containing membranes. Using a range of biophysical techniques, we show that the endocytic cargo binding of AP2 is driven by its interaction with PtdIns4,5P(2)-containing membranes.
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What OpenQuestion 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 OpenQuestion graph.