Chaperoning transmembrane helices in the lipid bilayer

J Cell Biol. 2021 Jan 4;220(1):e202012041. doi: 10.1083/jcb.202012041.

Abstract

Elimination of membrane proteins often requires recognition of their transmembrane domains (TMDs) in the lipid bilayer. In this issue, Arines et al. (2020. J. Cell Biol.https://doi.org/10.1083/jcb.202001116) show that in Saccharomyces cerevisiae, the vacuole-associated Rsp5 ubiquitin ligase uses a TMD in substrate adaptor Ssh4 to recognize membrane helices in Ypq1, which targets this lysine transporter for lysosomal degradation during lysine starvation.

Publication types

  • Research Support, N.I.H., Intramural
  • Comment

MeSH terms

  • Ligases
  • Lipid Bilayers
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae Proteins* / genetics
  • Ubiquitin

Substances

  • Lipid Bilayers
  • Saccharomyces cerevisiae Proteins
  • Ubiquitin
  • Ligases