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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.

Pubmed ID: 11106728


  • Nakagawa T
  • Setou M
  • Seog D
  • Ogasawara K
  • Dohmae N
  • Takio K
  • Hirokawa N



Publication Data

November 10, 2000

Associated Grants


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