| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2029643 | Structure | 2014 | 10 Pages |
•Chemical shift perturbation and PRE data identify interaction sites on Arf1 and Fapp1•Sites on Fapp1 for Arf1 and PI4P minimally overlap, supporting coincidence detection•A model of Fapp1, Arf1, and PI4P interacting on a bicelle surface is been constructed
SummaryInteractions among ADP-ribosylation factors (ARFs), various adaptor proteins, and membrane lipids are essential for intracellular vesicle transport of a variety of cellular materials. Here, we present nuclear magnetic resonance (NMR)-based information on the nature of the interaction of yeast Arf1 (yArf1) and the pleckstrin homology (PH) domain of four-phosphate-adaptor protein 1 (Fapp1) as it occurs at a model membrane surface. Interactions favor a model in which Fapp1 is partially embedded in the membrane and interacts with a membrane-associated Arf1 molecule primarily through contacts between residues in switch I of Arf1 and regions near and under the solution exposed C-terminal extension of the PH domain. The Arf1 binding site on Fapp1-PH is distinct from a positively charged phosphatidylinositol-4-phosphate (PI4P) binding site. A structural model is constructed that supports coincidence detection of both activated ARF and PI4P as a mechanism facilitating Fapp1 recruitment to membranes.
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