ArticleeLife2014
The membrane-associated proteins FCHo and SGIP are allosteric activators of the AP2 clathrin adaptor complex.
Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
What it found
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Who cites it
66 citing papers in PubMed, 98 citations in OpenAlex.
- NECAP antagonizes light-induced Rhodopsin-1 internalization to promote photoreceptor homeostasis.bioRxiv : the preprint server for biology · 2026Article
- FCHO1 fine-tunes synaptic vesicle endocytosis in an activity-dependent manner.Molecular brain · 2026Article
- Membrane Curvature and Cancer: Mechanisms, Implications, and Therapeutic Perspectives.Cancers · 2026Review
- Regulation of AP1 adaptor assembly by the bi-handed chaperone MEA1.Nature communications · 2026Article
- Integrating endogenous TurboID and data-independent acquisition mass spectrometry for in vivo proximity labeling.The EMBO journal · 2026Article
- Of condensates and coats - reciprocal regulation of clathrin assembly and the growth of protein networks.Nature communications · 2025Article
- Bi-handed assembly chaperones regulate protein complex assembly through an intramolecular handover mechanism.Science advances · 2025Article
- Of condensates and coats - reciprocal regulation of clathrin assembly and the growth of protein networks.bioRxiv : the preprint server for biology · 2025Article
- A structure-based mechanism for initiation of AP-3 coated vesicle formation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Intersectin1 promotes clathrin-mediated endocytosis by organizing and stabilizing endocytic protein interaction networks.Cell reports · 2024Article
- Intersectin1 promotes clathrin-mediated endocytosis by organizing and stabilizing endocytic protein interaction networks.Cell reports · 2024Article
- An AAGAB-to-CCDC32 handover mechanism controls the assembly of the AP2 adaptor complex.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Imaging Interorganelle Phospholipid Transport by Extended Synaptotagmins Using Bioorthogonally Tagged Lipids.ACS chemical biology · 2024Article
- Article
- A structure-based mechanism for initiation of AP-3 coated vesicle formation.bioRxiv : the preprint server for biology · 2024Article
- SGIP1 binding to the α-helical H9 domain of cannabinoid receptor 1 promotes axonal surface expression.Journal of cell science · 2024Article
- Intersectin1 promotes clathrin-mediated endocytosis by organizing and stabilizing endocytic protein interaction networks.bioRxiv : the preprint server for biology · 2024Article
- Biomolecular condensation orchestrates clathrin-mediated endocytosis in plants.Nature cell biology · 2024Article
- Dissecting membrane interfacial cellular processes: an in vitro reconstitution approach.The European physical journal. Special topics · 2024Review
- A suppressor screenProceedings of the National Academy of Sciences of the United States of America · 2023Article
6 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
11 authors at 4 institutions in 2 countries.
Funding
Abstract
The AP2 clathrin adaptor complex links protein cargo to the endocytic machinery but it is unclear how AP2 is activated on the plasma membrane. Here we demonstrate that the membrane-associated proteins FCHo and SGIP1 convert AP2 into an open, active conformation. We screened for Caenorhabditis elegans mutants that phenocopy the loss of AP2 subunits and found that AP2 remains inactive in fcho-1 mutants. A subsequent screen for bypass suppressors of fcho-1 nulls identified 71 compensatory mutations in all four AP2 subunits. Using a protease-sensitivity assay we show that these mutations restore the open conformation in vivo. The domain of FCHo that induces this rearrangement is not the F-BAR domain or the µ-homology domain, but rather is an uncharacterized 90 amino acid motif, found in both FCHo and SGIP proteins, that directly binds AP2. Thus, these proteins stabilize nascent endocytic pits by exposing membrane and cargo binding sites on AP2.
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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.