ArticleNature communications2024
An extended interaction site determines binding between AP180 and AP2 in clathrin mediated endocytosis.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed.
- CCDC32 collaborates with the membrane to assemble the AP-2 clathrin adaptor complex.Science advances · 2026Article
- Single-cell transcriptome profiling reveals herpesviral manipulation of host processes in spleen of gibel carp infected with a Cyvirus cyprinidallo2.PLoS pathogens · 2026Article
- Article
- Of condensates and coats - reciprocal regulation of clathrin assembly and the growth of protein networks.Nature communications · 2025Article
- Integrative cardiovascular disease therapy: Linoleic acid restriction, enhanced external counterpulsation, and emerging nanotherapies.World journal of cardiology · 2025Review
- Epsin1 enforces a condensation-dependent checkpoint for ubiquitylated cargo during clathrin-mediated endocytosis.Nature communications · 2025Article
- Promiscuous and multivalent interactions between Eps15 and partner protein Dab2 generate a complex interaction network.Nature communications · 2025Article
- The biomechanical phenomena observed in the cell invasion pathway of porcine epidemic diarrhea virus: a review.Archives of virology · 2025Review
- Of condensates and coats - reciprocal regulation of clathrin assembly and the growth of protein networks.bioRxiv : the preprint server for biology · 2025Article
- Bipartite binding of the intrinsically disordered scaffold protein JIP1 to the kinase JNK1.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Shared transcriptional regulators and network rewiring identify therapeutic targets linking type 2 diabetes mellitus and hypertension.Frontiers in molecular biosciences · 2025Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
The early phases of clathrin mediated endocytosis are organized through a highly complex interaction network mediated by clathrin associated sorting proteins (CLASPs) that comprise long intrinsically disordered regions (IDRs). AP180 is a CLASP exclusively expressed in neurons and comprises a long IDR of around 600 residues, whose function remains partially elusive. Using NMR spectroscopy, we discovered an extended and strong interaction site within AP180 with the major adaptor protein AP2, and describe its binding dynamics at atomic resolution. We find that the 70 residue-long site determines the overall interaction between AP180 and AP2 in a dynamic equilibrium between its bound and unbound states, while weaker binding sites contribute to the overall affinity at much higher concentrations of AP2. Our data suggest that this particular interaction site might play a central role in recruitment of adaptors to the clathrin coated pit, whereas more transient and promiscuous interactions allow reshaping of the interaction network until cargo uptake inside a coated vesicle.
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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 Socratic graph.