Microtubules-associated intracellular localization of the NH2-terminal cellular prion protein fragment |
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Authors: | Hachiya Naomi S Watanabe Kota Sakasegawa Yuji Kaneko Kiyotoshi |
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Affiliation: | Department of Cortical Function Disorders, National Institute of Neuroscience, National Center of Neurology and Psychiatry, Tokyo 187-8502, Japan. |
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Abstract: | By utilizing double-labeled fluorescent cellular prion protein (PrPC), 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 PrPC 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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Keywords: | Prion protein Microtubules Fluorescent protein Nocodazole Proteolytic cleavage Subcellular localization |
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