Please use this identifier to cite or link to this item: https://doi.org/10.1128/MCB.01719-08
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dc.titleTopology of mammalian isoprenylcysteine carboxyl methyltransferase determined in live cells with a fluorescent probe
dc.contributor.authorWright, L.P
dc.contributor.authorCourt, H
dc.contributor.authorMor, A
dc.contributor.authorAhearn, I.M
dc.contributor.authorCasey, P.J
dc.contributor.authorPhilips, M.R
dc.date.accessioned2020-10-27T06:54:00Z
dc.date.available2020-10-27T06:54:00Z
dc.date.issued2009
dc.identifier.citationWright, L.P, Court, H, Mor, A, Ahearn, I.M, Casey, P.J, Philips, M.R (2009). Topology of mammalian isoprenylcysteine carboxyl methyltransferase determined in live cells with a fluorescent probe. Molecular and Cellular Biology 29 (7) : 1826-1833. ScholarBank@NUS Repository. https://doi.org/10.1128/MCB.01719-08
dc.identifier.issn02707306
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/181012
dc.description.abstractIsoprenylcysteine carboxyl methyltransferase (Icmt) is a highly conserved enzyme that methyl esterifies the a carboxyl group of prenylated proteins including Ras and related GTPases. Methyl esterification neutralizes the negative charge of the prenylcysteine and thereby increases membrane affinity. Icmt is an integral membrane protein restricted to the endoplasmic reticulum (ER). The Saccharomyces cerevisiae ortholog, Ste14p, traverses the ER membrane six times. We used a novel fluorescent reporter to map the topology of human Icmt in living cells. Our results indicate that Icmt traverses the ER membrane eight times, with both N and C termini disposed toward the cytosol and with a helix-turn-helix structure comprising transmembrane (TM) segments 7 and 8. Several conserved amino acids that map to cytoplasmic portions of the enzyme are critical for full enzymatic activity. Mammalian Icmt has an N-terminal extension consisting of two TM segments not found in Ste14p and therefore likely to be regulatory. Icmt is a target for anticancer drug discovery, and these data may facilitate efforts to develop small-molecule inhibitors. Copyright © 2009, American Society for Microbiology.
dc.rightsAttribution 4.0 International
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.sourceUnpaywall 20201031
dc.subjectamino acid
dc.subjectcyan fluorescent protein
dc.subjectprotein s isoprenylcysteine o methyltransferase
dc.subjectasparagine
dc.subjectfluorescent dye
dc.subjectmutant protein
dc.subjectproline
dc.subjectprotein methyltransferase
dc.subjectprotein s isoprenylcysteine o methyltransferase
dc.subjectprotein-S-isoprenylcysteine O-methyltransferase
dc.subjectanimal cell
dc.subjectarticle
dc.subjectcontrolled study
dc.subjectcytoplasm
dc.subjectcytosol
dc.subjectembryo
dc.subjectendoplasmic reticulum
dc.subjectenzyme activity
dc.subjectenzyme localization
dc.subjecthuman
dc.subjecthuman cell
dc.subjectnonhuman
dc.subjectpriority journal
dc.subjectprotein structure
dc.subjectamino acid substitution
dc.subjectanimal
dc.subjectcell strain COS1
dc.subjectcell survival
dc.subjectCercopithecus
dc.subjectchemistry
dc.subjectenzymology
dc.subjectglycosylation
dc.subjectkinetics
dc.subjectmetabolism
dc.subjectnucleotide sequence
dc.subjectprotein secondary structure
dc.subjectprotein tertiary structure
dc.subjectMammalia
dc.subjectSaccharomyces cerevisiae
dc.subjectAmino Acid Substitution
dc.subjectAnimals
dc.subjectAsparagine
dc.subjectCell Survival
dc.subjectCercopithecus aethiops
dc.subjectConserved Sequence
dc.subjectCOS Cells
dc.subjectCytosol
dc.subjectEndoplasmic Reticulum
dc.subjectFluorescent Dyes
dc.subjectGlycosylation
dc.subjectHumans
dc.subjectKinetics
dc.subjectMutant Proteins
dc.subjectProline
dc.subjectProtein Methyltransferases
dc.subjectProtein Structure, Secondary
dc.subjectProtein Structure, Tertiary
dc.typeArticle
dc.contributor.departmentDUKE-NUS MEDICAL SCHOOL
dc.description.doi10.1128/MCB.01719-08
dc.description.sourcetitleMolecular and Cellular Biology
dc.description.volume29
dc.description.issue7
dc.description.page1826-1833
dc.published.statePublished
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