Ypt protein prenylation depends on the interplay among levels of Rab escort protein and geranylgeranyl diphosphate in yeast cells
Autor: | Wolfgang Wagner, Antonella Ragnini, Bettina E. Bauer, Marta Miaczynska, Rudolf J. Schweyen |
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Rok vydání: | 2001 |
Předmět: |
Geranylgeranyl Transferase
Saccharomyces cerevisiae Proteins Protein Prenylation Bioengineering yeast Biology Applied Microbiology and Biotechnology Biochemistry Geranylgeranylation Polyisoprenyl Phosphates Prenylation Yeasts lipid metabolism Genetics Settore BIO/10 disease Alkyl and Aryl Transferases traffico intracellulare lipid metabolism disease yeast prenyltransferase anticancer drugs Transport protein Cell biology Vesicular transport protein anticancer drugs rab GTP-Binding Proteins Mutation prenyltransferase Protein prenylation Rab Ras superfamily traffico intracellulare Biotechnology |
Zdroj: | Yeast. 18:697-709 |
ISSN: | 1097-0061 0749-503X |
DOI: | 10.1002/yea.719 |
Popis: | Farnesyl diphosphate (FPP), an intermediate of the sterol biosynthetic pathway, is used by farnesyl transferase to farnesylate, among others, the Ras proteins, and by geranylgeranyl diphosphate synthase to produce geranylgeranyl diphosphate (GGPP). GGPP is then transferred by geranylgeranyl transferase II (GGTase II) to Rab/Ypt members of the Ras superfamily known to be required at all stages of vesicle transport in both mammals and yeast. Formation of a complex between a Rab/Ypt protein and an accessory protein named the Rab escort protein (REP) is a prerequisite for GGTase II substrate recognition. Little is known about the factors that regulate GGTase II activity in living cells but, based on available data, it seems possible that vesicle transport in higher eukaryotes is regulated by the levels of prenylated Rab/Ypt proteins in the cells. Here we show that the levels of REP play an important role in regulating GGTase II activity in yeast cells if sufficient substrates are present. Moreover, overexpression of REP causes, directly or indirectly, an increased level of Ypt substrates available for prenylation, which in turn leads to the depletion of the GGPP pool in the cell. Overall our data suggest that the levels of REP and the availability of GGPP play a role in regulating Ypt protein prenylation. |
Databáze: | OpenAIRE |
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