The PX domain as a novel phosphoinositide-binding module

Tetsuro Ago, Ryu Takeya, Hidekazu Hiroaki, Futoshi Kuribayashi, Takashi Ito, Daisuke Kohda, Hideki Sumimoto

研究成果: ジャーナルへの寄稿記事

85 引用 (Scopus)

抄録

The phox (phagocyte oxidase) homology (PX) domain occurs in the mammalian phox proteins p40phox and p47phox, the polarity establishment protein Bem1p in budding yeast, and a variety of proteins involved in membrane trafficking. Here we show that the PX domains of p40phox and p47phox directly bind to phosphoinositides: p40phox prefers Ptdlns(3)P, while p47phox does Ptdlns(4)P and Ptdlns(3,4)P2. In addition, the Bem1p PX domain also interacts with Ptdlns(4)P. When the p40phox PX domain is expressed as a fusion to green fluorescent protein in HeLa cells, it exists at early endosomes where Ptdlns(3)P is enriched. Furthermore, a mutant p40phox PX carrying the substitution of Lys for Arg105 only weakly binds to phosphoinositides in vitro, and fails to locate to early endosomes. Thus the PX domain functions as a novel phosphoinositide-binding module and likely participates in targeting of proteins to membranes.

元の言語英語
ページ(範囲)733-738
ページ数6
ジャーナルBiochemical and Biophysical Research Communications
287
発行部数3
DOI
出版物ステータス出版済み - 9 28 2001

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Phosphatidylinositols
Endosomes
Phagocytes
Oxidoreductases
Proteins
Membranes
Saccharomycetales
Protein Transport
Green Fluorescent Proteins
HeLa Cells
Yeast
Membrane Proteins
Substitution reactions
Fusion reactions
neutrophil cytosol factor 40K

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

The PX domain as a novel phosphoinositide-binding module. / Ago, Tetsuro; Takeya, Ryu; Hiroaki, Hidekazu; Kuribayashi, Futoshi; Ito, Takashi; Kohda, Daisuke; Sumimoto, Hideki.

:: Biochemical and Biophysical Research Communications, 巻 287, 番号 3, 28.09.2001, p. 733-738.

研究成果: ジャーナルへの寄稿記事

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abstract = "The phox (phagocyte oxidase) homology (PX) domain occurs in the mammalian phox proteins p40phox and p47phox, the polarity establishment protein Bem1p in budding yeast, and a variety of proteins involved in membrane trafficking. Here we show that the PX domains of p40phox and p47phox directly bind to phosphoinositides: p40phox prefers Ptdlns(3)P, while p47phox does Ptdlns(4)P and Ptdlns(3,4)P2. In addition, the Bem1p PX domain also interacts with Ptdlns(4)P. When the p40phox PX domain is expressed as a fusion to green fluorescent protein in HeLa cells, it exists at early endosomes where Ptdlns(3)P is enriched. Furthermore, a mutant p40phox PX carrying the substitution of Lys for Arg105 only weakly binds to phosphoinositides in vitro, and fails to locate to early endosomes. Thus the PX domain functions as a novel phosphoinositide-binding module and likely participates in targeting of proteins to membranes.",
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AU - Ago, Tetsuro

AU - Takeya, Ryu

AU - Hiroaki, Hidekazu

AU - Kuribayashi, Futoshi

AU - Ito, Takashi

AU - Kohda, Daisuke

AU - Sumimoto, Hideki

PY - 2001/9/28

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N2 - The phox (phagocyte oxidase) homology (PX) domain occurs in the mammalian phox proteins p40phox and p47phox, the polarity establishment protein Bem1p in budding yeast, and a variety of proteins involved in membrane trafficking. Here we show that the PX domains of p40phox and p47phox directly bind to phosphoinositides: p40phox prefers Ptdlns(3)P, while p47phox does Ptdlns(4)P and Ptdlns(3,4)P2. In addition, the Bem1p PX domain also interacts with Ptdlns(4)P. When the p40phox PX domain is expressed as a fusion to green fluorescent protein in HeLa cells, it exists at early endosomes where Ptdlns(3)P is enriched. Furthermore, a mutant p40phox PX carrying the substitution of Lys for Arg105 only weakly binds to phosphoinositides in vitro, and fails to locate to early endosomes. Thus the PX domain functions as a novel phosphoinositide-binding module and likely participates in targeting of proteins to membranes.

AB - The phox (phagocyte oxidase) homology (PX) domain occurs in the mammalian phox proteins p40phox and p47phox, the polarity establishment protein Bem1p in budding yeast, and a variety of proteins involved in membrane trafficking. Here we show that the PX domains of p40phox and p47phox directly bind to phosphoinositides: p40phox prefers Ptdlns(3)P, while p47phox does Ptdlns(4)P and Ptdlns(3,4)P2. In addition, the Bem1p PX domain also interacts with Ptdlns(4)P. When the p40phox PX domain is expressed as a fusion to green fluorescent protein in HeLa cells, it exists at early endosomes where Ptdlns(3)P is enriched. Furthermore, a mutant p40phox PX carrying the substitution of Lys for Arg105 only weakly binds to phosphoinositides in vitro, and fails to locate to early endosomes. Thus the PX domain functions as a novel phosphoinositide-binding module and likely participates in targeting of proteins to membranes.

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