The common phospholipid-binding activity of the N-terminal domains of PEX1 and VCP/p97.

@article{Shiozawa2006TheCP,
  title={The common phospholipid-binding activity of the N-terminal domains of PEX1 and VCP/p97.},
  author={Kumiko Shiozawa and Natsuko Goda and Toshiyuki Shimizu and Kenji Mizuguchi and Naomi Kondo and Nobuyuki Shimozawa and Masahiro Shirakawa and Hidekazu Hiroaki},
  journal={The FEBS journal},
  year={2006},
  volume={273 21},
  pages={
          4959-71
        }
}
  • Kumiko Shiozawa, Natsuko Goda, +5 authors Hidekazu Hiroaki
  • Published in The FEBS journal 2006
  • Biology, Medicine
  • 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… CONTINUE READING

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