Enlargement of the endoplasmic reticulum membrane in Saccharomyces cerevisiae is not necessarily linked to the unfolded protein response via Ire1p

FEBS Letters

Tabak, Henk F¹  van den Berg, Marlene¹  Stroobants, An K¹  Hettema, Ewald H¹ 

[1] Department of Biochemistry, Academic Medical Centre, Meibergdreef 15, 1105 AZ Amsterdam, The Netherlands

关键词: Unfolded protein response;    Karmella;    Peroxisome biogenesis;    INO1;    Hmg1p;    hydroxy-methyl-glutaryl-CoA reductase iso-enzyme 1;    GFP;    green fluorescent protein;    UAS;    upstream activating sequence;   

DOI  :  10.1016/S0014-5793(99)00721-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown