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Differential fates of invertase mutants in the yeast endoplasmic reticulum

✍ Scribed by McCracken, Ardythe A.; Werner, Eric D.; Powell, Marguerite J.; Kruse, Kristina B.; Brodsky, Jeffrey L.

Publisher
John Wiley and Sons
Year
2000
Tongue
English
Weight
111 KB
Volume
16
Category
Article
ISSN
0749-503X

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✦ Synopsis

A number of proteins have been identi®ed 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 secretiondefective 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 de®cient in vacuolar protease activity and, additionally, we showed that Suc2-538p was stabilized in ERAD-de®cient strains, demonstrating that Suc2-538p was a substrate for ERAD.

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