Article
Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast.
Molecular biology of the cell - 1 Nov 2004
Youker Robert T, Walsh Peter, Beilharz Traude, Lithgow Trevor, Brodsky Jeffrey L
Abstract excerpt
Aberrant secreted proteins can be destroyed by ER-associated protein degradation (ERAD), and a prominent, medically relevant ERAD substrate is the cystic fibrosis transmembrane conductance regulator (CFTR). To better define the chaperone requirements during CFTR maturation, the protein was expressed in yeast. Because Hsp70 function impacts CFTR biogenesis in yeast and mammals, we first sought ER-associated Hsp40...
Topics
- Amino Acid Sequence
- Animals
- Cystic Fibrosis Transmembrane Conductance Regulator
- Genetic Techniques
- Genotype
- HSP40 Heat-Shock Proteins
- HSP90 Heat-Shock Proteins
- Heat-Shock Proteins
- Humans
- Hydrolysis
- Microscopy, Fluorescence
- Molecular Chaperones