Anterograde and retrograde intracellular trafficking of fluorescent cellular prion protein

Naomi S. Hachiya, Kota Watanabe, Makiko Yamada, Yuji Sakasegawa, Kiyotoshi Kaneko

Research output: Contribution to journalArticlepeer-review

40 Citations (Scopus)

Abstract

In order to investigate the microtubule-associated intracellular trafficking of the NH2-terminal cellular prion protein (PrPC) fragment [Biochem. Biophys. Res. Commun. 313 (2004) 818], we performed a real-time imaging of fluorescent PrPC (GFP-PrPC) in living cells. Such GFP-PrPC exhibited an anterograde movement towards the direction of plasma membranes at a speed of 140-180nm/s, and a retrograde movement inwardly at a speed of 1.0-1.2μm/s. The anterograde and retrograde movements of GFP-PrPC were blocked by a kinesin family inhibitor (AMP-PNP) and a dynein family inhibitor (vanadate), respectively. Furthermore, anti-kinesin antibody (α-kinesin) blocked its anterograde motility, whereas anti-dynein antibody (α-dynein) blocked its retrograde motility. These data suggested the kinesin family-driven anterograde and the dynein-driven retrograde movements of GFP-PrPC. Mapping of the interacting domains of PrPC identified amino acid residues indispensable for interactions with kinesin family: NH2-terminal mouse (Mo) residues 53-91 and dynein: NH2-terminal Mo residues 23-33, respectively. Our findings argue that the discrete N-terminal amino acid residues are indispensable for the anterograde and retrograde intracellular movements of PrPC.

Original languageEnglish
Pages (from-to)802-807
Number of pages6
JournalBiochemical and biophysical research communications
Volume315
Issue number4
DOIs
Publication statusPublished - 2004 Mar 19

Keywords

  • Cellular prion protein
  • Dynein
  • Green fluorescent protein
  • Kinesin family
  • Microtubules

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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