Futoshi Kuribayashi
   Department     ,
Article types 原著
Language English
Peer review Peer reviewed
Title The PX domain as a novel phosphoinositide- binding module.
Journal Formal name:Biochemical and biophysical research communications
Abbreviation:Biochem. Biophys. Res. Commun.
ISSN code:0006-291X (Print)
Volume, Issue, Page 287(3),733-738頁
Author and coauthor Ago Tetsuro, Takeya Ryu, Hiroaki Hidekazu, Kuribayashi Futoshi, Ito Takashi, Kohda Daisuke, Sumimoto Hideki.
Publication date 2002/09
Summary The phox (phagocyte oxidase) homology (PX) domain occurs in the mammalian phox proteins p40(phox) and p47(phox), 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 p40(phox) and p47(phox) directly bind to phosphoinositides: p40(phox) prefers Ptdlns(3)P, while p47(phox) does Ptdlns(4)P and Ptdlns(3,4)P(2). In addition, the Bem1p PX domain also interacts with Ptdlns(4)P. When the p40(phox) 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 p40(phox) 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.