Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adaptor Protein Complex alpha Subunits
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Adaptor Protein Complex beta Subunits
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Adaptor Proteins, Vesicular Transport
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Animals
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Binding Sites
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Carrier Proteins / genetics
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Carrier Proteins / metabolism*
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Cell Compartmentation
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Cell Fractionation
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Cell Membrane / metabolism*
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Cells, Cultured
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Fluorescent Antibody Technique
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Gene Library
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Intracellular Membranes / metabolism
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Kinesins / genetics
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Kinesins / metabolism*
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Membrane Proteins / metabolism*
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Mice
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Microscopy, Immunoelectron
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Molecular Motor Proteins / metabolism*
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Molecular Sequence Data
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Movement
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Precipitin Tests
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Protein Binding
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Protein Structure, Tertiary
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Protein Transport
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Receptor, IGF Type 2 / metabolism*
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Recombinant Proteins / biosynthesis
Substances
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Adaptor Protein Complex alpha Subunits
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Adaptor Protein Complex beta Subunits
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Adaptor Proteins, Vesicular Transport
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Carrier Proteins
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KIF13A protein, human
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Membrane Proteins
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Molecular Motor Proteins
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Receptor, IGF Type 2
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Recombinant Proteins
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Kinesins