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

@article{Jensen1995MultiplePS,
  title={Multiple proteolytic systems, including the proteasome, contribute to CFTR processing},
  author={Timothy J. Jensen and Melinda A. Loo and Steven Pind and David B. Williams and Alfred L Goldberg and John R. Riordan},
  journal={Cell},
  year={1995},
  volume={83},
  pages={129-135}
}
The molecular components of the quality control system that rapidly degrades abnormal membrane and secretory proteins have not been identified. The cystic fibrosis transmembrane conductance regulator (CFTR) is an integral membrane protein to which this quality control is stringently applied; approximately 75% of the wild-type precursor and 100% of the delta F508 CFTR variant found in most CF patients are rapidly degraded before exiting from the ER. We now show that this ER degradation is… CONTINUE READING
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Functions of the proteasome: the lysis at the end of the tunnel

A. L. Goldberg
Science • 1995
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