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A novel motor, KIF13A, transports mannose-6-phosphate receptor to plasma membrane through direct interaction with AP-1 complex.

Cell | Nov 10, 2000

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.

Pubmed ID: 11106728 RIS Download

Mesh terms: Adaptor Protein Complex alpha Subunits | Adaptor Protein Complex beta Subunits | Adaptor Proteins, Vesicular Transport | Animals | Binding Sites | Carrier Proteins | Cell Compartmentation | Cell Fractionation | Cell Membrane | Cells, Cultured | Fluorescent Antibody Technique | Gene Library | Intracellular Membranes | Kinesin | Membrane Proteins | Mice | Microscopy, Immunoelectron | Molecular Motor Proteins | Molecular Sequence Data | Movement | Precipitin Tests | Protein Binding | Protein Structure, Tertiary | Protein Transport | Receptor, IGF Type 2 | Recombinant Proteins

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