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

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

doi:10.1016/j.bbrc.2003.11.167

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

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

MED - United Centers for Advanced Research and Translational Medicine (ART)

Research output: Contribution to journal › Article › peer-review

35 Citations (Scopus)

Abstract

By utilizing double-labeled fluorescent cellular prion protein (PrP ^C), we revealed that the NH₂-terminal and COOH-terminal PrP^C 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 PrP^C 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 PrP^C fragment containing at least the 1-91 amino acid residues.

Original language	English
Pages (from-to)	818-823
Number of pages	6
Journal	Biochemical and biophysical research communications
Volume	313
Issue number	3
DOIs	https://doi.org/10.1016/j.bbrc.2003.11.167
Publication status	Published - 2004 Jan 16

Keywords

Fluorescent protein
Microtubules
Nocodazole
Prion protein
Proteolytic cleavage
Subcellular localization

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2003.11.167

Cite this

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title = "Microtubules-associated intracellular localization of the NH 2-terminal cellular prion protein fragment",

abstract = "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.",

keywords = "Fluorescent protein, Microtubules, Nocodazole, Prion protein, Proteolytic cleavage, Subcellular localization",

author = "Hachiya, {Naomi S.} and Kota Watanabe and Yuji Sakasegawa and Kiyotoshi Kaneko",

note = "Funding Information: We greatly thank S.B. Prusiner and D.A. Harris for discussions and comments, T. Onodera for providing us the HpL3-4 cell line, M. Kawabata, E. Nannri, C. Ota, and Y. Yamaura for technical assistances. This work was supported by grants from the Core Research for Evolutional Science and Technology (CREST) of Japan Science and Technology Agency, Health and Labour Sciences Research Grants, Research on Advanced Medical Technology, nano-001, and the Ministry of Health, Labor, and Welfare of Japan.",

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AU - Hachiya, Naomi S.

AU - Watanabe, Kota

AU - Sakasegawa, Yuji

AU - Kaneko, Kiyotoshi

N1 - Funding Information: We greatly thank S.B. Prusiner and D.A. Harris for discussions and comments, T. Onodera for providing us the HpL3-4 cell line, M. Kawabata, E. Nannri, C. Ota, and Y. Yamaura for technical assistances. This work was supported by grants from the Core Research for Evolutional Science and Technology (CREST) of Japan Science and Technology Agency, Health and Labour Sciences Research Grants, Research on Advanced Medical Technology, nano-001, and the Ministry of Health, Labor, and Welfare of Japan.

PY - 2004/1/16

Y1 - 2004/1/16

N2 - 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.

AB - 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.

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KW - Subcellular localization

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