DOI:10.1016/S0092-8674(02)00735-3 - Corpus ID: 483953
Molecular Architecture and Functional Model of the Endocytic AP2 Complex
@article{Collins2002MolecularAA, title={Molecular Architecture and Functional Model of the Endocytic AP2 Complex}, author={Brett M. Collins and Airlie J. McCoy and Helen M. Kent and Philip R. Evans and David. J. Owen}, journal={Cell}, year={2002}, volume={109}, pages={523-535}, url={https://api.semanticscholar.org/CorpusID:483953}}- B. CollinsA. McCoyD. Owen
- Published inCell17 May 2002
- Biology, Chemistry
628 Citations
628 Citations
A structural mechanism for phosphorylation-dependent inactivation of the AP2 complex
- E. PartlowR. W. BakerGwendolyn M. BeachamJ. ChappieA. LeschzinerG. Hollopeter
- 2019
Biology, Chemistry
High-resolution cryo-EM structures of NECAP bound to phosphorylated AP2 are reported and it is proposed that phosphorylation marks adaptors for inactivation.
Tyrosine-based endocytic motifs stimulate oligomerization of AP-2 adaptor complexes.
It is reported here that soluble tyrosine-based endocytic sorting motif peptides facilitate clathrin/AP-2 recruitment to liposomal membranes and induce adaptor oligomerization even in the absence of a lipid bilayer.
Recognition of a Basic AP-2 Binding Motif within the C2B Domain of Synaptotagmin Is Dependent on Multimerization*
- Isabelle GrassS. ThielS. HöningV. Haucke
- 2004
Biology, Chemistry
It is hypothesized that basic motifs within multimeric membrane proteins may represent a novel type of clathrin/AP-2-dependent endocytosis signal.
A structure-based mechanism for initiation of AP-3 coated vesicle formation
- Matthew BegleyMahira F. AragonRichard W. Baker
- 2024
Biology, Chemistry
This study provides a structural mechanism for the recruitment and initial polymerization of AP-3, which mediates cargo sorting in tubular and recycling endosomes, and proposes that Arf1 and AP-3 collaborate to form clathrin-independent coats in the endosomal compartment.
Crystal structure of the clathrin adaptor protein 1 core.
- E. HeldweinE. MaciaJing WangH. YinT. KirchhausenS. Harrison
- 2004
Biology, Chemistry
The crystal structure of the core of the AP-1 complex, which functions in the trans-Golgi network (TGN), is reported and it is shown that directed mutations of residues at a particular corner of the gamma chain prevent recruitment to the TGN in cells and diminish PI-4-P- dependent, but not Arf1-dependent, liposome binding in vitro.
Functional Analysis of AP-2 α and μ2 Subunits
- A. MotleyNicola BergM. Robinson
- 2006
Biology, Chemistry
There is some functional redundancy in the binding sites of the various AP-2 subunits, because no single mutation totally abolishes function, and a new model system is established that can be used both for additional structure-function analyses, and as a way of testing tagged constructs for function in vivo.
The μ2 Subunit of the Clathrin Adaptor AP‐2 Binds to FDNPVY and YppØ Sorting Signals at Distinct Sites
- W. BollIris RapoportC. BrunnerY. ModisS. PrehnT. Kirchhausen
- 2002
Biology, Chemistry
The results suggest the possibility that low‐density lipoprotein receptor uptake may be modulated specifically and independently of other proteins in the clathrin pathway.
NECAPs are negative regulators of the AP2 clathrin adaptor complex
This work reports that loss of ncap-1, the sole C. elegans gene encoding an adaptiN Ear-binding Coat-Associated Protein (NECAP), bypasses the requirement for FCHO-1 and proposes NECAPs function late in endocytosis to inactivate AP2.
Conserved structural motifs in intracellular trafficking pathways: structure of the gammaCOP appendage domain.
- G. HoffmanP. RahlR. CollinsR. Cerione
- 2003
Biology, Chemistry
A structural explanation for the binding of endocytic dileucine motifs by the AP2 complex
- Bernard T. KellyA. McCoyD. Owen
- 2008
Biology, Chemistry
Most transmembrane proteins are selected as transport-vesicle cargo through the recognition of short, linear amino-acid motifs in their cytoplasmic portions by vesicle coat proteins. For…
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74 References
Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly.
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Biology, Chemistry
Structural-based mutagenesis shows that alterations to the molecular surface of a highly conserved region on the platform domain differentially affect associations of the appendage with amphiphysin, eps15,epsin, and AP180, revealing a common protein-binding interface.
Regulatory interactions in the recognition of endocytic sorting signals by AP‐2 complexes
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Biology, Chemistry
The findings indicate that receptor recruitment can be coupled to clathrin coat assembly and suggest a mechanism for regulation of membrane traffic by lipid products of phosphoinositide 3‐kinases.
Phosphorylation of threonine 156 of the μ2 subunit of the AP2 complex is essential for endocytosis in vitro and in vivo
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Biology
Sequence requirements for the recognition of tyrosine‐based endocytic signals by clathrin AP‐2 complexes.
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Biology, Chemistry
It is concluded that sorting into the endocytic pathway is governed by a surprisingly simple interaction between the mu 2 chain and a tyrosine‐containing tetrapeptide sequence.
Phosphoinositide–Ap-2 Interactions Required for Targeting to Plasma Membrane Clathrin-Coated Pits
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Biology, Chemistry
It is suggested that phosphoinositides play a critical and general role in adaptor incorporation into plasma membrane clathrin-coated pits and ligand-dependent recruitment of arrestin-receptor complexes to coated pits.
Targeting signals and subunit interactions in coated vesicle adaptor complexes
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Biology, Chemistry
The results indicate that the adaptor subunits act in concert to target the complex to the appropriate membrane.
A structural explanation for the recognition of tyrosine-based endocytotic signals.
Crystal structures of the internalization signal binding domain of mu2 complexed with theinternalization signal peptides of epidermal growth factor receptor and the trans-Golgi network protein TGN38 have been determined at 2.7 angstrom resolution.
Binding of AP2 to Sorting Signals Is Modulated by AP2 Phosphorylation*
- A. FingerhutK. von FiguraS. Höning
- 2001
Biology, Chemistry
A cycle of phosphorylation/dephosphorylation as a mechanism for regulating the reversible association of AP2 with membranes and sorting signals during the process of receptor-mediated endocytosis is shown.
Simultaneous binding of PtdIns(4,5)P2 and clathrin by AP180 in the nucleation of clathrin lattices on membranes.
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- 2001
Biology, Chemistry
The structure of the NH2-terminal domain of CALM bound to phosphatidylinositol-4,5- bisphosphate [PtdIns( 4,5)P2] via a lysine-rich motif is presented, and it is shown that AP180 may serve to tether clathrin to the membrane simultaneously, and was shown by using purified components and a budding assay on preformed lipid monolayers.
The structure and function of the β2‐adaptin appendage domain
- David J. OwenY. VallisBarbara M.F. PearseHarvey T. McMahonPhilip R. Evans
- 2000
Biology, Chemistry
Using structure‐directed mutagenesis, the ability of the β2 appendage alone to bind directly to clathrin and the accessory proteins AP180, epsin and eps15 at the same site is demonstrated.
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