A Novel Motor, KIF13A, Transports Mannose-6-Phosphate Receptor to Plasma Membrane through Direct Interaction with AP-1 Complex
Copyright policy )A Novel Motor, KIF13A, Transports Mannose-6-Phosphate Receptor to Plasma Membrane through Direct Interaction with AP-1 Complex
Intracellular transport mediated by kinesin superfamily proteins (KIFs) is a highly regulated process. The molecular mechanism of KIFs binding to their respective cargoes remains unclear. We report that KIF13A is a novel plus end-directed microtubule-dependent motor protein and associates with beta 1-adaptin, a subunit of the AP-1 adaptor complex. The cargo vesicles of KIF13A contained AP-1 and mannnose-6-phosphate receptor (M6PR). Overexpression of KIF13A resulted in mislocalization of the AP-1 and the M6PR. Functional blockade of KIF13A reduced cell surface expression of the M6PR. Thus, KIF13A transports M6PR-containing vesicles and targets the M6PR from TGN to the plasma membrane via direct interaction with the AP-1 adaptor complex.
- University of Tokyo Japan
- RIKEN Japan
Binding Sites, Biochemistry, Genetics and Molecular Biology(all), Molecular Motor Proteins, Movement, Cell Membrane, Molecular Sequence Data, Fluorescent Antibody Technique, Kinesins, Membrane Proteins, Intracellular Membranes, Cell Fractionation, Cell Compartmentation, Adaptor Proteins, Vesicular Transport, Mice, Adaptor Protein Complex alpha Subunits, Animals, Adaptor Protein Complex beta Subunits, Carrier Proteins, Microscopy, Immunoelectron, Cells, Cultured, Gene Library
Binding Sites, Biochemistry, Genetics and Molecular Biology(all), Molecular Motor Proteins, Movement, Cell Membrane, Molecular Sequence Data, Fluorescent Antibody Technique, Kinesins, Membrane Proteins, Intracellular Membranes, Cell Fractionation, Cell Compartmentation, Adaptor Proteins, Vesicular Transport, Mice, Adaptor Protein Complex alpha Subunits, Animals, Adaptor Protein Complex beta Subunits, Carrier Proteins, Microscopy, Immunoelectron, Cells, Cultured, Gene Library
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