The Ankrd13 Family of Ubiquitin-interacting Motif-bearing Proteins Regulates Valosin-containing Protein/p97 Protein-mediated Lysosomal Trafficking of Caveolin 1.

@article{Burana2016TheAF,
  title={The Ankrd13 Family of Ubiquitin-interacting Motif-bearing Proteins Regulates Valosin-containing Protein/p97 Protein-mediated Lysosomal Trafficking of Caveolin 1.},
  author={Daocharad Burana and Hidehito Yoshihara and Hidetaka Tanno and Akitsugu Yamamoto and Yasushi Saeki and Keiji Tanaka and Masayuki Komada},
  journal={The Journal of biological chemistry},
  year={2016},
  volume={291 12},
  pages={6218-31}
}
Caveolin 1 (Cav-1) is an oligomeric protein that forms flask-shaped, lipid-rich pits, termed caveolae, on the plasma membrane. Cav-1 is targeted for lysosomal degradation in ubiquitination- and valosin-containing protein (VCP)-dependent manners. VCP, an ATPase associated with diverse cellular activities that remodels or segregates ubiquitinated protein complexes, has been proposed to disassemble Cav-1 oligomers on the endosomal membrane, facilitating the trafficking of Cav-1 to the lysosome… CONTINUE READING

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