• Register
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.


Leaving Community

Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.


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