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- Title
The common phospholipid-binding activity of the N-terminal domains of PEX1 and VCP/p97.
- Authors
Shiozawa, Kumiko; Goda, Natsuko; Shimizu, Toshiyuki; Mizuguchi, Kenji; Kondo, Naomi; Shimozawa, Nobuyuki; Shirakawa, Masahiro; Hiroaki, Hidekazu
- Abstract
PEX1 is a type II AAA-ATPase that is indispensable for biogenesis and maintenance of the peroxisome, an organelle responsible for the primary metabolism of lipids, such as beta-oxidation and lipid biosynthesis. Recently, we demonstrated a striking structural similarity between its N-terminal domain and those of other membrane-related AAA-ATPases, such as valosine-containing protein (p97). The N-terminal domain of valosine-containing protein serves as an interface to its adaptor proteins p47 and Ufd1, whereas the physiologic interaction partner of the N-terminal domain of PEX1 remains unknown. Here we found that N-terminal domains isolated from valosine-containing protein, as well as from PEX1, bind phosphoinositides. The N-terminal domain of PEX1 appears to preferentially bind phosphatidylinositol 3-monophosphate and phosphatidylinositol 4-monophosphate, whereas the N-terminal domain of valosine-containing protein displays broad and nonspecific lipid binding. Although N-ethylmaleimide-sensitive fusion protein, CDC48 and Ufd1 have structures similar to that of valosine-containing protein, they displayed lipid specificity similar to that of the N-terminal domain of PEX1 in the assays. By mutational analysis, we demonstrate that a conserved arginine surrounded by hydrophobic residues is essential for lipid binding, despite very low sequence similarity between PEX1 and valosine-containing protein.
- Publication
The FEBS journal, 2006, Vol 273, Issue 21, p4959
- ISSN
1742-464X
- Publication type
Journal Article
- DOI
10.1111/j.1742-4658.2006.05494.x