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Enlargement of the endoplasmic reticulum membrane in Saccharomyces cerevisiae is not necessarily linked to the unfolded protein response via Ire1p
Author(s) -
Stroobants An K,
Hettema Ewald H,
van den Berg Marlene,
Tabak Henk F
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00721-8
Subject(s) - endoplasmic reticulum , unfolded protein response , saccharomyces cerevisiae , inositol , protein folding , chemistry , biochemistry , microbiology and biotechnology , protein biosynthesis , biosynthesis , biology , enzyme , yeast , receptor
Conditions that stress the endoplasmic reticulum (ER) in Saccharomyces cerevisiae can elicit a combination of an unfolded protein response (UPR) and an inositol response (IR). This results in increased synthesis of ER protein‐folding factors and of enzymes participating in phospholipid biosynthesis. It was suggested that in cells grown on glucose or galactose medium, the UPR and the IR are linked and controlled by the ER stress sensor Ire1p. However, our studies suggest that during growth on oleate the IR is controlled both by an Ire1p‐dependent pathway and by an Ire1p‐independent pathway.