Structural basis for recognition of ubiquitinated cargo by Tom1-GAT domain

Masato Akutsu; Masato Kawasaki; Yohei Katoh; Tomoo Shiba; Yoshiki Yamaguchi; Ryuichi Kato; Koichi Kato; Kazuhisa Nakayama; Soichi Wakatsuki

doi:10.1016/j.febslet.2005.08.076

Structural basis for recognition of ubiquitinated cargo by Tom1-GAT domain

Masato Akutsu, Masato Kawasaki, Yohei Katoh, Tomoo Shiba, Yoshiki Yamaguchi, Ryuichi Kato, Koichi Kato, Kazuhisa Nakayama, Soichi Wakatsuki

研究成果: Article › 査読

28 被引用数 (Scopus)

抄録

Tom1 (Target of Myb1) is suggested to be involved in the transport of ubiquitinated proteins, through the interaction of its GAT (GGA and Tom1) domain with ubiquitin. Here, we demonstrate that the three-helix bundle of Tom1-GAT has two ubiquitin-binding sites recognizing the hydrophobic Ile44 surface of ubiquitin. The complex crystal structure demonstrates that the first site is a hydrophobic patch on helices α1 and α2. NMR and biochemical data revealed that the N-terminal half of helix α3 of Tom1-GAT constitutes the second, stronger binding site. The double-sided ubiquitin binding enhances the efficiency of recognition of ubiquitinated proteins by Tom1.

本文言語	English
ページ（範囲）	5385-5391
ページ数	7
ジャーナル	FEBS Letters
巻	579
号	24
DOI	https://doi.org/10.1016/j.febslet.2005.08.076
出版ステータス	Published - 2005 10月 10
外部発表	はい

ASJC Scopus subject areas

生物理学
構造生物学
生化学
分子生物学
遺伝学
細胞生物学

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10.1016/j.febslet.2005.08.076

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title = "Structural basis for recognition of ubiquitinated cargo by Tom1-GAT domain",

abstract = "Tom1 (Target of Myb1) is suggested to be involved in the transport of ubiquitinated proteins, through the interaction of its GAT (GGA and Tom1) domain with ubiquitin. Here, we demonstrate that the three-helix bundle of Tom1-GAT has two ubiquitin-binding sites recognizing the hydrophobic Ile44 surface of ubiquitin. The complex crystal structure demonstrates that the first site is a hydrophobic patch on helices α1 and α2. NMR and biochemical data revealed that the N-terminal half of helix α3 of Tom1-GAT constitutes the second, stronger binding site. The double-sided ubiquitin binding enhances the efficiency of recognition of ubiquitinated proteins by Tom1.",

keywords = "GGA and Tom1, Golgi-localizing, γ-adaptin ear domain homology, ARF-binding, Protein transport, Target of Myb1, Ubiquitin recognition",

author = "Masato Akutsu and Masato Kawasaki and Yohei Katoh and Tomoo Shiba and Yoshiki Yamaguchi and Ryuichi Kato and Koichi Kato and Kazuhisa Nakayama and Soichi Wakatsuki",

note = "Funding Information: We thank Y. Kito for her help in the preparation of recombinant proteins for NMR spectroscopy. This work was supported by Protein 3000 project and by Grants-in-Aid from the Ministry of Education, Culture, Sports, Science and Technology of Japan.",

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T1 - Structural basis for recognition of ubiquitinated cargo by Tom1-GAT domain

AU - Akutsu, Masato

AU - Kawasaki, Masato

AU - Katoh, Yohei

AU - Shiba, Tomoo

AU - Yamaguchi, Yoshiki

AU - Kato, Ryuichi

AU - Kato, Koichi

AU - Nakayama, Kazuhisa

AU - Wakatsuki, Soichi

N1 - Funding Information: We thank Y. Kito for her help in the preparation of recombinant proteins for NMR spectroscopy. This work was supported by Protein 3000 project and by Grants-in-Aid from the Ministry of Education, Culture, Sports, Science and Technology of Japan.

PY - 2005/10/10

Y1 - 2005/10/10

N2 - Tom1 (Target of Myb1) is suggested to be involved in the transport of ubiquitinated proteins, through the interaction of its GAT (GGA and Tom1) domain with ubiquitin. Here, we demonstrate that the three-helix bundle of Tom1-GAT has two ubiquitin-binding sites recognizing the hydrophobic Ile44 surface of ubiquitin. The complex crystal structure demonstrates that the first site is a hydrophobic patch on helices α1 and α2. NMR and biochemical data revealed that the N-terminal half of helix α3 of Tom1-GAT constitutes the second, stronger binding site. The double-sided ubiquitin binding enhances the efficiency of recognition of ubiquitinated proteins by Tom1.

AB - Tom1 (Target of Myb1) is suggested to be involved in the transport of ubiquitinated proteins, through the interaction of its GAT (GGA and Tom1) domain with ubiquitin. Here, we demonstrate that the three-helix bundle of Tom1-GAT has two ubiquitin-binding sites recognizing the hydrophobic Ile44 surface of ubiquitin. The complex crystal structure demonstrates that the first site is a hydrophobic patch on helices α1 and α2. NMR and biochemical data revealed that the N-terminal half of helix α3 of Tom1-GAT constitutes the second, stronger binding site. The double-sided ubiquitin binding enhances the efficiency of recognition of ubiquitinated proteins by Tom1.

KW - GGA and Tom1

KW - Golgi-localizing, γ-adaptin ear domain homology, ARF-binding

KW - Protein transport

KW - Target of Myb1

KW - Ubiquitin recognition

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Structural basis for recognition of ubiquitinated cargo by Tom1-GAT domain

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