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Related Experiment Videos

Multiple proteolytic systems, including the proteasome, contribute to CFTR processing

T J Jensen1, M A Loo, S Pind

  • 1S. C. Johnson Medical Research Center, Mayo Clinic Scottsdale, Arizona 85259, USA.

Cell
|October 6, 1995
PubMed
Summary
This summary is machine-generated.

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The endoplasmic reticulum (ER) quality control system rapidly degrades abnormal proteins. Researchers found that the cystic fibrosis transmembrane conductance regulator (CFTR) protein is degraded by the cytosolic proteasome during ER maturation.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Protein Degradation

Background:

  • The endoplasmic reticulum (ER) possesses a quality control system for degrading misfolded membrane and secretory proteins.
  • The cystic fibrosis transmembrane conductance regulator (CFTR) is an integral membrane protein that is subject to stringent ER quality control.
  • Most wild-type CFTR precursors (~75%) and all delta F508 CFTR variants (~100%) are degraded before ER exit.

Purpose of the Study:

  • To identify the molecular components responsible for the rapid degradation of abnormal membrane and secretory proteins.
  • To investigate the role of the cytosolic proteasome in the ER-associated degradation of CFTR.

Main Methods:

  • Treatment of cells with proteasome inhibitors, including lactacystin and peptide aldehydes (e.g., MG-132).

Related Experiment Videos

  • Assessment of CFTR precursor degradation and maturation.
  • Analysis of ATP-dependent conformational changes in CFTR.

    • Main Results:

    • ER degradation of CFTR is sensitive to cytosolic proteasome inhibitors.
    • MG-132 inhibits the degradation of CFTR precursor and blocks its ATP-dependent folding.
    • CFTR and other membrane proteins are substrates for proteasomal degradation during ER maturation.

    Conclusions:

    • The cytosolic proteasome is involved in the ER quality control and degradation of CFTR.
    • Proteasomal degradation occurs during the maturation of CFTR and likely other integral membrane proteins within the ER.