Role of NH2-terminal hydrophobic motif in the subcellular localization of ATP-binding cassette protein subfamily D: Common features in eukaryotic organisms

Asaka Lee; Kota Asahina; Takumi Okamoto; Kosuke Kawaguchi; Dzmitry G. Kostsin; Yoshinori Kashiwayama; Kojiro Takanashi; Kazufumi Yazaki; Tsuneo Imanaka; Masashi Morita

doi:10.1016/j.bbrc.2014.09.133

Role of NH₂-terminal hydrophobic motif in the subcellular localization of ATP-binding cassette protein subfamily D: Common features in eukaryotic organisms

Asaka Lee, Kota Asahina, Takumi Okamoto, Kosuke Kawaguchi, Dzmitry G. Kostsin, Yoshinori Kashiwayama, Kojiro Takanashi, Kazufumi Yazaki, Tsuneo Imanaka^*, Masashi Morita

^*Corresponding author for this work

Molecular Cell Biology

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

11 Scopus citations

Abstract

In mammals, four ATP-binding cassette (ABC) proteins belonging to subfamily D have been identified. ABCD1-3 possesses the NH₂-terminal hydrophobic region and are targeted to peroxisomes, while ABCD4 lacking the region is targeted to the endoplasmic reticulum (ER). Based on hydropathy plot analysis, we found that several eukaryotes have ABCD protein homologs lacking the NH₂-terminal hydrophobic segment (H0 motif). To investigate whether the role of the NH₂-terminal H0 motif in subcellular localization is conserved across species, we expressed ABCD proteins from several species (metazoan, plant and fungi) in fusion with GFP in CHO cells and examined their subcellular localization. ABCD proteins possessing the NH₂-terminal H0 motif were localized to peroxisomes, while ABCD proteins lacking this region lost this capacity. In addition, the deletion of the NH₂-terminal H0 motif of ABCD protein resulted in their localization to the ER. These results suggest that the role of the NH₂-terminal H0 motif in organelle targeting is widely conserved in living organisms.

Original language	English
Pages (from-to)	612-618
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	453
Issue number	3
DOIs	https://doi.org/10.1016/j.bbrc.2014.09.133
State	Published - 2014/10/24

Keywords

ABC protein subfamily D
Endoplasmic reticulum
Peroxisome
Secretory pathway
Targeting

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2014.09.133

Cite this

Lee, A., Asahina, K., Okamoto, T., Kawaguchi, K., Kostsin, D. G., Kashiwayama, Y., Takanashi, K., Yazaki, K., Imanaka, T., & Morita, M. (2014). Role of NH₂-terminal hydrophobic motif in the subcellular localization of ATP-binding cassette protein subfamily D: Common features in eukaryotic organisms. Biochemical and Biophysical Research Communications, 453(3), 612-618. https://doi.org/10.1016/j.bbrc.2014.09.133

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title = "Role of NH2-terminal hydrophobic motif in the subcellular localization of ATP-binding cassette protein subfamily D: Common features in eukaryotic organisms",

abstract = "In mammals, four ATP-binding cassette (ABC) proteins belonging to subfamily D have been identified. ABCD1-3 possesses the NH2-terminal hydrophobic region and are targeted to peroxisomes, while ABCD4 lacking the region is targeted to the endoplasmic reticulum (ER). Based on hydropathy plot analysis, we found that several eukaryotes have ABCD protein homologs lacking the NH2-terminal hydrophobic segment (H0 motif). To investigate whether the role of the NH2-terminal H0 motif in subcellular localization is conserved across species, we expressed ABCD proteins from several species (metazoan, plant and fungi) in fusion with GFP in CHO cells and examined their subcellular localization. ABCD proteins possessing the NH2-terminal H0 motif were localized to peroxisomes, while ABCD proteins lacking this region lost this capacity. In addition, the deletion of the NH2-terminal H0 motif of ABCD protein resulted in their localization to the ER. These results suggest that the role of the NH2-terminal H0 motif in organelle targeting is widely conserved in living organisms.",

keywords = "ABC protein subfamily D, Endoplasmic reticulum, Peroxisome, Secretory pathway, Targeting",

author = "Asaka Lee and Kota Asahina and Takumi Okamoto and Kosuke Kawaguchi and Kostsin, {Dzmitry G.} and Yoshinori Kashiwayama and Kojiro Takanashi and Kazufumi Yazaki and Tsuneo Imanaka and Masashi Morita",

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Lee, A, Asahina, K, Okamoto, T, Kawaguchi, K, Kostsin, DG, Kashiwayama, Y, Takanashi, K, Yazaki, K, Imanaka, T & Morita, M 2014, 'Role of NH₂-terminal hydrophobic motif in the subcellular localization of ATP-binding cassette protein subfamily D: Common features in eukaryotic organisms', Biochemical and Biophysical Research Communications, vol. 453, no. 3, pp. 612-618. https://doi.org/10.1016/j.bbrc.2014.09.133

Role of NH₂-terminal hydrophobic motif in the subcellular localization of ATP-binding cassette protein subfamily D: Common features in eukaryotic organisms. / Lee, Asaka; Asahina, Kota; Okamoto, Takumi et al.
In: Biochemical and Biophysical Research Communications, Vol. 453, No. 3, 24.10.2014, p. 612-618.

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

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T1 - Role of NH2-terminal hydrophobic motif in the subcellular localization of ATP-binding cassette protein subfamily D

T2 - Common features in eukaryotic organisms

AU - Lee, Asaka

AU - Asahina, Kota

AU - Okamoto, Takumi

AU - Kawaguchi, Kosuke

AU - Kostsin, Dzmitry G.

AU - Kashiwayama, Yoshinori

AU - Takanashi, Kojiro

AU - Yazaki, Kazufumi

AU - Imanaka, Tsuneo

AU - Morita, Masashi

PY - 2014/10/24

Y1 - 2014/10/24

N2 - In mammals, four ATP-binding cassette (ABC) proteins belonging to subfamily D have been identified. ABCD1-3 possesses the NH2-terminal hydrophobic region and are targeted to peroxisomes, while ABCD4 lacking the region is targeted to the endoplasmic reticulum (ER). Based on hydropathy plot analysis, we found that several eukaryotes have ABCD protein homologs lacking the NH2-terminal hydrophobic segment (H0 motif). To investigate whether the role of the NH2-terminal H0 motif in subcellular localization is conserved across species, we expressed ABCD proteins from several species (metazoan, plant and fungi) in fusion with GFP in CHO cells and examined their subcellular localization. ABCD proteins possessing the NH2-terminal H0 motif were localized to peroxisomes, while ABCD proteins lacking this region lost this capacity. In addition, the deletion of the NH2-terminal H0 motif of ABCD protein resulted in their localization to the ER. These results suggest that the role of the NH2-terminal H0 motif in organelle targeting is widely conserved in living organisms.

AB - In mammals, four ATP-binding cassette (ABC) proteins belonging to subfamily D have been identified. ABCD1-3 possesses the NH2-terminal hydrophobic region and are targeted to peroxisomes, while ABCD4 lacking the region is targeted to the endoplasmic reticulum (ER). Based on hydropathy plot analysis, we found that several eukaryotes have ABCD protein homologs lacking the NH2-terminal hydrophobic segment (H0 motif). To investigate whether the role of the NH2-terminal H0 motif in subcellular localization is conserved across species, we expressed ABCD proteins from several species (metazoan, plant and fungi) in fusion with GFP in CHO cells and examined their subcellular localization. ABCD proteins possessing the NH2-terminal H0 motif were localized to peroxisomes, while ABCD proteins lacking this region lost this capacity. In addition, the deletion of the NH2-terminal H0 motif of ABCD protein resulted in their localization to the ER. These results suggest that the role of the NH2-terminal H0 motif in organelle targeting is widely conserved in living organisms.

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KW - Secretory pathway

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