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    Elimination of defective alpha-factor pheromone receptors

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    Authors
    Jenness, Duane D.
    Li, Yu
    Tipper, Christopher
    Spatrick, Phyllis
    UMass Chan Affiliations
    Department of Molecular Genetics and Microbiology
    Graduate School of Biomedical Sciences
    Document Type
    Journal Article
    Publication Date
    1997-10-29
    Keywords
    Biological Transport; Cell Compartmentation; Cell Membrane; Cloning, Molecular; Fungal Proteins; Models, Molecular; Mutation; Protein Conformation; Protein Folding; Receptors, Mating Factor; Receptors, Peptide; Reproduction; Saccharomyces cerevisiae; Sequence Analysis, DNA; *Transcription Factors; Vacuoles
    Life Sciences
    Medicine and Health Sciences
    
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    Link to Full Text
    https://www.ncbi.nlm.nih.gov/pmc/articles/PMC232474/
    Abstract
    This report compares trafficking routes of a plasma membrane protein that was misfolded either during its synthesis or after it had reached the cell surface. A temperature-sensitive mutant form of the yeast alpha-factor pheromone receptor (ste2-3) was found to provide a model substrate for quality control of plasma membrane proteins. We show for the first time that a misfolded membrane protein is recognized at the cell surface and rapidly removed. When the ste2-3 mutant cells were cultured continuously at 34 degrees C, the mutant receptor protein (Ste2-3p) failed to accumulate at the plasma membrane and was degraded with a half-life of 4 min, compared with a half-life of 33 min for wild-type receptor protein (Ste2p). Degradation of both Ste2-3p and Ste2p required the vacuolar proteolytic activities controlled by the PEP4 gene. At 34 degrees C, Ste2-3p comigrated with glycosylated Ste2p on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, indicating that Ste2-3p enters the secretory pathway. Degradation of Ste2-3p did not require delivery to the plasma membrane as the sec1 mutation failed to block rapid turnover. Truncation of the C-terminal cytoplasmic domain of the mutant receptors did not permit accumulation at the plasma membrane; thus, the endocytic signals contained in this domain are unnecessary for intracellular retention. In the pep4 mutant, Ste2-3p accumulated as series of high-molecular-weight species, suggesting a potential role for ubiquitin in the elimination process. When ste2-3 mutant cells were cultured continuously at 22 degrees C, Ste2-3p accumulated in the plasma membrane. When the 22 degrees C culture was shifted to 34 degrees C, Ste2-3p was removed from the plasma membrane and degraded by a PEP4-dependent mechanism with a 24-min half-life; the wild-type Ste2p displayed a 72-min half-life. Thus, structural defects in Ste2-3p synthesized at 34 degrees C are recognized in transit to the plasma membrane, leading to rapid degradation, and Ste2-3p that is preassembled at the plasma membrane is also removed and degraded following a shift to 34 degrees C.
    Source

    Mol Cell Biol. 1997 Nov;17(11):6236-45.

    DOI
    10.1128/MCB.17.11.6236
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/33933
    PubMed ID
    9343384
    Related Resources

    Link to article in PubMed

    ae974a485f413a2113503eed53cd6c53
    10.1128/MCB.17.11.6236
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