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Identification of a mitochondrial targeting sequence in cathepsin D and its localization in mitochondria

Naoki Ikari, View ORCID ProfileHirofumi Arakawa
doi: https://doi.org/10.1101/2023.01.23.524639
Naoki Ikari
Division of Cancer Biology, National Cancer Center Research Institute, 5-1-1 Tsukiji, Chuo-ku, Tokyo, Japan
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Hirofumi Arakawa
Division of Cancer Biology, National Cancer Center Research Institute, 5-1-1 Tsukiji, Chuo-ku, Tokyo, Japan
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  • ORCID record for Hirofumi Arakawa
  • For correspondence: harakawa@ncc.go.jp
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Abstract

Cathepsin D (CTSD) is a major lysosomal protease harboring an N-terminal signal peptide (amino acids 1–20) to enable vesicular transport from endoplasmic reticulum to lysosomes. Here, we report the possibility of a mitochondrial targeting sequence and mitochondrial localization of CTSD in cells. Live-cell imaging analysis with enhanced green fluorescent protein (EGFP)-CTSD indicated that CTSD localizes to mitochondria. CTSD amino acids 21–35 are responsible for its mitochondrial localization, which exhibit typical features of mitochondrial targeting sequences, and are evolutionarily conserved. A proteinase K protection assay and sucrose gradient analysis showed that a small population of endogenous CTSD molecules exists in mitochondria. These results suggest that CTSD is a dual-targeted protein that may localize in both lysosomes and mitochondria.

Competing Interest Statement

The authors have declared no competing interest.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission.
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Posted January 24, 2023.
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Identification of a mitochondrial targeting sequence in cathepsin D and its localization in mitochondria
Naoki Ikari, Hirofumi Arakawa
bioRxiv 2023.01.23.524639; doi: https://doi.org/10.1101/2023.01.23.524639
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Identification of a mitochondrial targeting sequence in cathepsin D and its localization in mitochondria
Naoki Ikari, Hirofumi Arakawa
bioRxiv 2023.01.23.524639; doi: https://doi.org/10.1101/2023.01.23.524639

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