ArticleChembiochem : a European journal of chemical biology2008
Protein farnesyltransferase-catalyzed isoprenoid transfer to peptide depends on lipid size and shape, not hydrophobicity.
Article in Chembiochem : a European journal of chemical biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 24 citations in OpenAlex.
- BicyclicInternational journal of molecular sciences · 2025Article
- Promiscuous Enzymes for Residue-Specific Peptide and Protein Late-Stage Functionalization.Chembiochem : a European journal of chemical biology · 2023Review
- Protein Farnesyltransferase Catalyzes Unanticipated Farnesylation and Geranylgeranylation of Shortened Target Sequences.Biochemistry · 2020Article
- Structure and specificity of a permissive bacterial C-prenyltransferase.Nature chemical biology · 2017Article
- Formation of a Novel Macrocyclic Alkaloid from the Unnatural Farnesyl Diphosphate Analogue Anilinogeranyl Diphosphate by 5-Epi-Aristolochene Synthase.ACS chemical biology · 2015Article
- Design and synthesis of non-hydrolyzable homoisoprenoid α-monofluorophosphonate inhibitors of PPAPDC family integral membrane lipid phosphatases.Bioorganic & medicinal chemistry letters · 2014Article
- Site-specific labeling of proteins and peptides with trans-cyclooctene containing handles capable of tetrazine ligation.Chemical biology & drug design · 2014Article
- Engineering protein farnesyltransferase for enzymatic protein labeling applications.Bioconjugate chemistry · 2014Article
- Identification of a farnesol analog as a Ras function inhibitor using both an in vivo Ras activation sensor and a phenotypic screening approach.Molecular and cellular biochemistry · 2014Article
- Simultaneous dual protein labeling using a triorthogonal reagent.Journal of the American Chemical Society · 2013Article
- Farnesyl diphosphate analogues with aryl moieties are efficient alternate substrates for protein farnesyltransferase.Biochemistry · 2012Article
- Synthesis of Farnesol Analogues Containing Triazoles in Place of Isoprenes through 'Click Chemistry'Synlett : accounts and rapid communications in synthetic organic chemistry · 2012Article
- Synthesis of frame-shifted farnesyl diphosphate analogs.Organic letters · 2012Article
- Chemoenzymatic reversible immobilization and labeling of proteins without prior purification.Journal of the American Chemical Society · 2012Article
- Lipid and sulfur substituted prenylcysteine analogs as human Icmt inhibitors.Bioorganic & medicinal chemistry letters · 2011Article
- Selective labeling of polypeptides using protein farnesyltransferase via rapid oxime ligation.Chemical communications (Cambridge, England) · 2010Article
- Novel Citronellyl-Based Photoprobes Designed to Identify ER Proteins Interacting with Dolichyl Phosphate in Yeast and Mammalian Cells.Current chemical biologyArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Protein farnesyl transferase (FTase) catalyzes transfer of a 15-carbon farnesyl group from farnesyl diphosphate (FPP) to a conserved cysteine in the C-terminal Ca(1)a(2)X motif of a range of proteins, including the oncoprotein H-Ras ("C" refers to the cysteine, "a" to any aliphatic amino acid, and "X" to any amino acid) and the lipid chain interacts with, and forms part of the Ca(1)a(2)X peptide binding site. Previous studies have shown that H-Ras biological function is ablated when it is modified with lipids that are 3-5 orders of magnitude less hydrophobic than FPP. Here, we employed a library of anilinogeranyl diphosphate (AGPP) and phenoxygeranyl diphosphate (PGPP) derivatives with a range of polarities (log P (lipid alcohol) = 0.7-6.8, log P (farnesol) = 6.1) and shapes to examine whether FTase-catalyzed transfer to peptide is dependent on the hydrophobicity of the lipid. Analysis of steady-state transfer kinetics for analogues to dansyl-GCVLS peptide revealed that the efficiency of lipid transfer was highly dependent on both the shape and size, but was independent of the polarity of the analogue. These observations indicate that hydrophobic features of isoprenoids critical for their association with membranes and/or protein receptors are not required for efficient transfer to Ca(1)a(2)X peptides by FTase. Furthermore, the results of these studies indicate that the role played by the farnesyl lipid in the FTase mechanism is primarily structural. To explain these results we propose a model in which the FTase active site stabilizes a membrane interface-like environment.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.