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Stefan Höning

Researcher at University of Cologne

Publications -  62
Citations -  5333

Stefan Höning is an academic researcher from University of Cologne. The author has contributed to research in topics: Clathrin & Endosome. The author has an hindex of 36, co-authored 59 publications receiving 4930 citations. Previous affiliations of Stefan Höning include Max Planck Society & University of Göttingen.

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A Large-Scale Conformational Change Couples Membrane Recruitment to Cargo Binding in the AP2 Clathrin Adaptor Complex

TL;DR: Using a range of biophysical techniques, it is shown that the endocytic cargo binding of AP2 is driven by its interaction with PtdIns4,5P2-containing membranes.
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A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3

TL;DR: Monitoring surface plasmon resonance observed that AP‐3 is able to interact with the tail of the lysosomal integral membrane protein LIMP‐II and that this binding depends on a DEXXXLI sequence in the LIMP-II tail, which points to a function of AP‐ 3 in intracellular sorting to lysoomes and melanosomes of a subset of cargo proteins via di‐leucine‐based sorting motifs.
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A structural explanation for the binding of endocytic dileucine motifs by the AP2 complex

TL;DR: In this paper, the crystal structure of AP2 in a complex with the diceucine motif of a cargo protein was presented, and the mechanism of cargo-adaptor recognition was revealed.
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Phosphatidylinositol-(4,5)-bisphosphate regulates sorting signal recognition by the clathrin-associated adaptor complex AP2.

TL;DR: It is demonstrated that recognition of Yxxvarphi and acidic dileucine motifs is dependent on corecognition with PtdIns4,5P(2), explaining the selective recruitment of AP2 to the plasma membrane.
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Phosphorylation of the AP2 μ subunit by AAK1 mediates high affinity binding to membrane protein sorting signals

TL;DR: It is proposed that phosphorylation of the AP2 μ2 subunit by AAK1 ensures high affinity binding of AP2 to sorting signals of cargo membrane proteins during the initial steps of receptor-mediated endocytosis.