Molecular architecture and functional model of the endocytic AP2 complex.

By B. Collins, A. McCoy, H. Kent, P. Evans, D. Owen. Cell, 2002

638 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/479876d112f7ef9744e94bc186822fdc572a0745

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Citations in the corpus

Regulated portals of entry into the cell (2003, background): “Analysis of high-resolution structures of isolated domains of coat proteins, culminating in the recently described structure of the AP2 core domai”
The Ark1/Prk1 family of protein kinases (2003, background): “AAK1 was identified as a binding partner for the appendage or ear domain of the α-adaptin component of AP2 complexes (Conner & Schmid, 2002).”
An introduction to stereochemical restraints (2006, background): “D63, 58–61 proteins, e.g. the AP2 complex (Collins et al., 2002), it is in the second (five equatorial, one axial) conformation (Fig.”
Molecular mechanism and physiological functions of clathrin-mediated endocytosis (2011, background): “AP2 binds both cargo and PtdIns(4,5)P 2 ; it interacts directly with motifs in the cytoplasmic tails of transmembrane receptors through its μ-subunit and σ-subunit, and indirectly with cargo using its appendage domains to bind accessory adaptor protein”
Functional Analysis of AP-2 α and μ2 Subunits (2006, background): “This indicates that the complex undergoes a conformational change, probably favored by phosphorylation of the 2 subunit, to flip out the 2 Cterminal subdomain (Collins et al., 2002).”
Rabaptin‐5α/rabaptin‐4 serves as a linker between rab4 and γ1‐adaptin in membrane recycling from endosomes (2003, background): “This tetrameric adaptor conceptually is a heterodimer of tightly bound a±s2 and b2±m2 subcomplexes (Collins et al., 2002).”
Solving structures of protein complexes by molecular replacement with Phaser (2006, background): “The structure of the endocytic AP2 complex was originally solved in space group P3121 (Collins et al., 2002).”