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Differential fates of invertase mutants in the yeast endoplasmic reticulum
Author(s) -
McCracken Ardythe A.,
Werner Eric D.,
Powell Marguerite J.,
Kruse Kristina B.,
Brodsky Jeffrey L.
Publication year - 2000
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/(sici)1097-0061(20000115)16:1<49::aid-yea506>3.0.co;2-i
Subject(s) - endoplasmic reticulum associated protein degradation , endoplasmic reticulum , biology , invertase , yeast , mutant , saccharomyces cerevisiae , protease , biochemistry , protein degradation , microbiology and biotechnology , unfolded protein response , enzyme , gene
A number of proteins have been identified as substrates for endoplasmic reticulum (ER)‐associated protein degradation (ERAD) and we describe here a new model substrate with which to study this process. Two secretion‐defective forms of yeast invertase that accumulated in the ER to greatly different levels were examined: Suc2‐538p levels were low, while Suc2‐533p was present in high amounts. Because Suc2‐533p and Suc2‐538p mRNA levels were comparable, we examined whether Suc2‐538p was targeted for degradation. Both mutant polypeptide levels were unaffected in a yeast strain deficient in vacuolar protease activity and, additionally, we showed that Suc2‐538p was stabilized in ERAD‐deficient strains, demonstrating that Suc2‐538p was a substrate for ERAD. Copyright © 2000 John Wiley & Sons, Ltd.