JOURNAL ARTICLE
RESEARCH SUPPORT, NON-U.S. GOV'T
REVIEW
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Dolichol biosynthesis in the yeast Saccharomyces cerevisiae: an insight into the regulatory role of farnesyl diphosphate synthase.

Dolichol, an isoprenoid lipid, known mainly for its function in protein glycosylation, is synthesised in the mevalonate pathway. The pathway is highly regulated, on multiple levels, by sterol and non-sterol derivatives of mevalonic acid. Farnesyl diphosphate (FPP) and/or FPP-derived molecules have been identified as the main non-sterol compounds regulating degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, one of the regulatory enzymes in the mevalonate pathway. In the present review we concentrate on the effect of overexpression of farnesyl diphosphate synthase on dolichol biosynthesis in yeast. In this context the role of the Yta7 protein, belonging to the AAA ATPase family, in the regulation of FPP flux to the dolichol branch of the mevalonate pathway is discussed, and the effect of FPP and/or derived molecules on the transcription of genes encoding the first enzyme committed to dolichol biosynthesis, i.e. cis-prenyl transferase.

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