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 K. 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}
}
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

Citations

Publications citing this paper.
Showing 1-9 of 9 extracted citations

The AAA+ superfamily--a myriad of motions.

Current opinion in structural biology • 2007
View 10 Excerpts
Highly Influenced

Cdc48: A Swiss Army Knife of Cell Biology

Journal of amino acids • 2013
View 1 Excerpt

References

Publications referenced by this paper.
Showing 1-10 of 70 references

Similar Papers

Loading similar papers…