Cargo-sorting signals promote polymerization of adaptor protein-1 in an Arf-1.GTP-independent manner |
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Authors: | Lee Intaek Drake Matthew T Traub Linton M Kornfeld Stuart |
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Institution: | a Department of Internal Medicine, Washington University School of Medicine, 660 South Euclid Avenue Box No. 8125, St. Louis, MO 63110, USA b Department of Endocrinology, Mayo Clinic, Rochester, MN 55905, USA c Department of Cell Biology and Physiology, University of Pittsburgh School of Medicine, PA 15261, USA |
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Abstract: | Adaptor protein-1 (AP-1) is recruited onto the trans-Golgi network via binding to Arf-1·GTP, cargo-sorting signals and phosphoinositides, where it orchestrates the assembly of clathrin-coated vesicular carriers that transport cargo molecules to endosomes. Here we show that cytosolic AP-1 polymerizes when recruited onto enriched Golgi membranes and liposomes containing covalently attached cargo-sorting signal peptides. Incubation of cytosolic or purified AP-1 with soluble sorting signal peptides also resulted in AP-1 polymerization, showing that Arf-1·GTP and membranes are not required for this process. We propose that cargo-induced polymerization of AP-1 contributes to stabilization of the coat complex in the formation of clathrin-coated buds. |
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Keywords: | Adaptor protein-1 Arf-1 Polymerization Golgi Cargo-sorting signals Tyrosine-sorting signals Di-leucine-sorting signals Peptidoliposomes |
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