Molecular Architecture and Functional Model of the Endocytic AP2 Complex
Open accessAbstract
AP2 is the best-characterized member of the family of heterotetrameric clathrin adaptor complexes that play pivotal roles in many vesicle trafficking pathways within the cell. AP2 functions in clathrin-mediated endocytosis, the process whereby cargo enters the endosomal system from the plasma membrane. We describe the structure of the 200 kDa AP2 "core" (alpha trunk, beta2 trunk, mu2, and sigma2) complexed with the polyphosphatidylinositol headgroup mimic inositolhexakisphosphate at 2.6 A resolution. Two potential polyphosphatidylinositide binding sites are observed, one on alpha and one on mu2. The binding site for Yxxphi endocytic motifs is buried, indicating that a conformational change, probably triggered by phosphorylation in the disordered mu2 linker, is necessary to allow Yxxphi motif binding. A model for AP2 recruitment and activation is proposed.
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CME requires the AP2 complex to recruit cargo proteins to endocytic vesicles.
“To recruit cargo proteins to endocytic vesicles, CME requires the heterotetrameric adaptor protein complex AP2 complex that acts as an adaptor between cargo proteins and clathrin coats (5, 15–18).”
From Regulation of cargo exocytosis by a Reps1-Ralbp1-RalA module (2023) · cites this paper as [17]
The Introduction (page unavailable) identifies AP2 as the predominant adaptor in clathrin-coated vesicles mediating CME and says it binds protein cargo. The Abstract (page unavailable) describes AP2 as a heterotetrameric clathrin adaptor. These passages support its adaptor role, but do not establish the stronger claim that CME requires AP2 to recruit cargo. (LLM, conf=0.83)
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- [1]1. Abrahams, J.P. ∙ Leslie, A.G.W. Methods used in the structure determination of bovine mitochondrial F1 ATPase Acta Crystallogr. D. 1996; 52:30-42 Crossref Scopus (1153) PubMed Google Scholar
- [2]2. Beck, K.A. ∙ Keen, J.H. Interaction of phosphoinositide cycle intermediates with the plasma membrane-associated clathrin assembly protein AP2 J. Biol. Chem. 1991; 266:4442-4447
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- Authors
- Collins, B. M., McCoy, A. J., Kent, H. M., Evans, P. R., & Owen, D. J.
- Affiliations
- University of Cambridge (GB)
- MRC Laboratory of Molecular Biology (GB)
- Corresponding author
- Owen, David J.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2002-05
- Volume
- 109
- Issue
- 4
- Pages
- 523-535
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2119260049
- Cited by
- 648
- References
- 0
- Citations by year
- 2026: 28 · 2025: 32 · 2024: 23 · 2023: 14 · 2022: 14 · 2021: 19 · 2020: 19 · 2019: 32 · 2018: 22 · 2017: 15 · 2016: 20 · 2015: 24 · 2014: 29 · 2013: 40 · 2012: 21
- FWCI
- 13.55
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 4095 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- AP-2, clathrin adaptor complexes, clathrin-mediated endocytosis, phytic acid, protein complex structure, vesicle trafficking
- MeSH terms
- Animals, Binding Sites, Carrier Proteins, Cell Membrane, Clathrin, Eukaryotic Cells, Humans, Membrane Proteins, Models, Biological, Phosphatidylinositols, Protein Binding, Molecular Structure, Protein Structure, Tertiary, Amino Acid Motifs, Protein Transport, Transport Vesicles, Adaptor Proteins, Vesicular Transport, Adaptor Protein Complex 1, Adaptor Protein Complex 2, Adaptor Protein Complex 3, Adaptor Protein Complex mu Subunits, Mice, Rats
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