Microtubules-associated intracellular localization of the NH 2-terminal cellular prion protein fragment

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

Research output: Contribution to journalArticlepeer-review

35 Citations (Scopus)


By utilizing double-labeled fluorescent cellular prion protein (PrP C), we revealed that the NH2-terminal and COOH-terminal PrPC fragments exhibit distinct distribution patterns in mouse neuroblastoma neuro2a (N2a) cells and HpL3-4, a hippocampal cell line established from prnp gene-ablated mice [Nature 400 (1999) 225]. Of note, the NH2-terminal PrPC fragment, which predominantly localized in the intracellular compartments, congregated in the cytosol after the treatment with a microtubule depolymerizer (nocodazole). Truncated PrP C with the amino acid residues 1-121, 1-111, and 1-91 in mouse (Mo) PrP exhibited a proper distribution profile, whereas those with amino acid residues 1-52 and 1-33 did not. These data indicate the microtubules-associated intracellular localization of the NH2-terminal PrPC fragment containing at least the 1-91 amino acid residues.

Original languageEnglish
Pages (from-to)818-823
Number of pages6
JournalBiochemical and biophysical research communications
Issue number3
Publication statusPublished - 2004 Jan 16


  • Fluorescent protein
  • Microtubules
  • Nocodazole
  • Prion protein
  • Proteolytic cleavage
  • Subcellular localization

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'Microtubules-associated intracellular localization of the NH 2-terminal cellular prion protein fragment'. Together they form a unique fingerprint.

Cite this