Protein quality control at the plasma membrane

Curr Opin Cell Biol. 2011 Aug;23(4):483-91. doi: 10.1016/ Epub 2011 May 14.


Cellular proteostasis (or protein homeostasis) depends on the timely folding and disposal of conformationally damaged polypeptides during their life span at all subcellular locations. This process is particularly important for membrane proteins confined to the cell surface with crucial regulatory role in cellular homoeostasis and intercellular communication. Accumulating evidences indicate that membrane proteins exported from the endoplasmic reticulum (ER) are subjected to peripheral quality control (QC) along the late secretory and endocytic pathways, as well as at the plasma membrane (PM). Recently identified components of the PM QC recognition and effector mechanisms responsible for ubiquitination and lysosomal degradation of conformationally damaged PM proteins uncovered striking similarities to and differences from that of the ER QC machinery. Possible implications of the peripheral protein QC activity in phenotypic modulation of conformational diseases are also outlined.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Cell Membrane / metabolism*
  • Endoplasmic Reticulum / metabolism
  • Humans
  • Lysosomes / metabolism
  • Mammals / metabolism
  • Membrane Proteins / metabolism*
  • Protein Transport*
  • Ubiquitination
  • Yeasts / cytology
  • Yeasts / metabolism


  • Membrane Proteins