Lipidation of BmAtg8 is required for autophagic degradation of p62 bodies containing ubiquitinated proteins in the silkworm, Bombyx mori

Ming Ming Ji, Man Lee, Hiroaki Mon, Kazuhiro Iiyama, Tsuneyuki Tatsuke, Daisuke Morokuma, Masato Hino, Mami Yamashita, Kazuma Hirata, Takahiro Kusakabe

研究成果: ジャーナルへの寄稿記事

3 引用 (Scopus)

抄録

p62/Sequestosome-1 (p62/SQSTM1, hereafter referred to as p62) is a major adaptor that allows ubiquitinated proteins to be degraded by autophagy, and Atg8 homologs are required for p62-mediated autophagic degradation, but their relationship is still not understood in Lepidopteran insects. Here it is clearly demonstrated that the silkworm homolog of mammalian p62, Bombyx mori p62 (Bmp62), forms p62 bodies depending on its Phox and Bem1p (PB1) and ubiquitin-associated (UBA) domains. These two domains are associated with Bmp62 binding to ubiquitinated proteins to form the p62 bodies, and the UBA domain is essential for the binding, but Bmp62 still self-associates without the PB1 or UBA domain. The p62 bodies in Bombyx cells are enclosed by BmAtg9-containing membranes and degraded via autophagy. It is revealed that the interaction between the Bmp62 AIM motif and BmAtg8 is critical for the autophagic degradation of the p62 bodies. Intriguingly, we further demonstrate that lipidation of BmAtg8 is required for the Bmp62-mediated complete degradation of p62 bodies by autophagy. Our results should be useful in future studies of the autophagic mechanism in Lepidopteran insects.

元の言語英語
ページ(範囲)86-96
ページ数11
ジャーナルInsect Biochemistry and Molecular Biology
89
DOI
出版物ステータス出版済み - 10 1 2017

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Ubiquitinated Proteins
Bombyx
Bombyx mori
Ubiquitin
silkworms
autophagy
Degradation
ubiquitin
degradation
Autophagy
proteins
Lepidoptera
Insects
insects
Membranes
4-ethoxymethylene-2-phenyl-2-oxazoline-5-one

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Insect Science

これを引用

Lipidation of BmAtg8 is required for autophagic degradation of p62 bodies containing ubiquitinated proteins in the silkworm, Bombyx mori. / Ji, Ming Ming; Lee, Man; Mon, Hiroaki; Iiyama, Kazuhiro; Tatsuke, Tsuneyuki; Morokuma, Daisuke; Hino, Masato; Yamashita, Mami; Hirata, Kazuma; Kusakabe, Takahiro.

:: Insect Biochemistry and Molecular Biology, 巻 89, 01.10.2017, p. 86-96.

研究成果: ジャーナルへの寄稿記事

Ji, Ming Ming ; Lee, Man ; Mon, Hiroaki ; Iiyama, Kazuhiro ; Tatsuke, Tsuneyuki ; Morokuma, Daisuke ; Hino, Masato ; Yamashita, Mami ; Hirata, Kazuma ; Kusakabe, Takahiro. / Lipidation of BmAtg8 is required for autophagic degradation of p62 bodies containing ubiquitinated proteins in the silkworm, Bombyx mori. :: Insect Biochemistry and Molecular Biology. 2017 ; 巻 89. pp. 86-96.
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abstract = "p62/Sequestosome-1 (p62/SQSTM1, hereafter referred to as p62) is a major adaptor that allows ubiquitinated proteins to be degraded by autophagy, and Atg8 homologs are required for p62-mediated autophagic degradation, but their relationship is still not understood in Lepidopteran insects. Here it is clearly demonstrated that the silkworm homolog of mammalian p62, Bombyx mori p62 (Bmp62), forms p62 bodies depending on its Phox and Bem1p (PB1) and ubiquitin-associated (UBA) domains. These two domains are associated with Bmp62 binding to ubiquitinated proteins to form the p62 bodies, and the UBA domain is essential for the binding, but Bmp62 still self-associates without the PB1 or UBA domain. The p62 bodies in Bombyx cells are enclosed by BmAtg9-containing membranes and degraded via autophagy. It is revealed that the interaction between the Bmp62 AIM motif and BmAtg8 is critical for the autophagic degradation of the p62 bodies. Intriguingly, we further demonstrate that lipidation of BmAtg8 is required for the Bmp62-mediated complete degradation of p62 bodies by autophagy. Our results should be useful in future studies of the autophagic mechanism in Lepidopteran insects.",
author = "Ji, {Ming Ming} and Man Lee and Hiroaki Mon and Kazuhiro Iiyama and Tsuneyuki Tatsuke and Daisuke Morokuma and Masato Hino and Mami Yamashita and Kazuma Hirata and Takahiro Kusakabe",
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AU - Iiyama, Kazuhiro

AU - Tatsuke, Tsuneyuki

AU - Morokuma, Daisuke

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AU - Kusakabe, Takahiro

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