Targeting Protein Prenylation in Progeria
نویسندگان
چکیده
منابع مشابه
Protein prenylation in spinach chloroplasts.
Protein prenylation in plants was studied by in vivo metabolic (3)H-mevalonate labeling in combination with a range of protein synthesis inhibitors. In spinach cotyledons, this posttranslational protein modification was found to be divided into two categories, one representing the conventional prenylation involving farnesyl and geranylgeranyl groups bound to cysteine residues via thioether link...
متن کاملBiochemistry of protein prenylation.
Covalent modification by isoprenoid lipids (prenylation) is now recognized as a mechanism to promote membrane interactions and biological activities of a variety of cellular proteins. Both the 15-carbon farnesyl and 20-carbon geranylgeranyl isoprenoids are involved in these modifications, which occur on carboxyl-terminal cysteine residues of proteins (Fig. 1). Known prenylated proteins include ...
متن کاملMechanisms of protein prenylation and role in G protein function.
Introduction Covalent attachment of isoprenoid lipids is now recognized as an important modification of many proteins involved in cellular signalling [ 1,2]. This type of modification, termed prenylation, involves attachment of either the 15-carbon farnesyl or 20carbon geranylgeranyl isoprenoid to C-terminal cysteine residues of proteins. Known prenylated proteins include a number of GTP-bindin...
متن کاملProtein farnesyltransferase and protein prenylation in Plasmodium falciparum.
Comparison of the malaria parasite and mammalian protein prenyltransferases and their cellular substrates is important for establishing this enzyme as a target for developing antimalarial agents. Nineteen heptapeptides differing only in their carboxyl-terminal amino acid were tested as alternative substrates of partially purified Plasmodium falciparum protein farnesyltransferase. Only NRSCAIM a...
متن کاملProtein prenylation: a pivotal posttranslational process.
The joining of the 15-carbon farnesyl group ðC15H25Þ and the 20-carbon geranylgeranyl group ðC20H33Þ to protein–cysteines at or near their carboxy-termini is catalyzed by protein farnesyltransferase (FTase) and protein geranylgeranyltransferase-I and II (GGTase-I and GGTase-II) [1]. The prenyltransferases are heterodimers consisting of aand b-subunits with combined molecular masses ranging from...
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ژورنال
عنوان ژورنال: Science Translational Medicine
سال: 2013
ISSN: 1946-6234,1946-6242
DOI: 10.1126/scitranslmed.3005229