Please use this identifier to cite or link to this item: https://doi.org/10.1242/jcs.200204
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dc.titlePredicting the targeting of tail-anchored proteins to subcellular compartments in mammalian cells
dc.contributor.authorCostello J.L.
dc.contributor.authorCastro I.G.
dc.contributor.authorCamões F.
dc.contributor.authorSchrader T.A.
dc.contributor.authorMcNeall D.
dc.contributor.authorYang J.
dc.contributor.authorGiannopoulou E.-A.
dc.contributor.authorGomes S.
dc.contributor.authorPogenberg V.
dc.contributor.authorBonekamp N.A.
dc.contributor.authorRibeiro D.
dc.contributor.authorWilmanns M.
dc.contributor.authorJedd G.
dc.contributor.authorIslinger M.
dc.contributor.authorSchrader M.
dc.date.accessioned2020-09-09T06:24:18Z
dc.date.available2020-09-09T06:24:18Z
dc.date.issued2017
dc.identifier.citationCostello J.L., Castro I.G., Camões F., Schrader T.A., McNeall D., Yang J., Giannopoulou E.-A., Gomes S., Pogenberg V., Bonekamp N.A., Ribeiro D., Wilmanns M., Jedd G., Islinger M., Schrader M. (2017). Predicting the targeting of tail-anchored proteins to subcellular compartments in mammalian cells. Journal of Cell Science 130 (9) : 1675-1687. ScholarBank@NUS Repository. https://doi.org/10.1242/jcs.200204
dc.identifier.issn0021-9533
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/175225
dc.description.abstractTail-anchored (TA) proteins contain a single transmembrane domain (TMD) at the C-terminus that anchors them to the membranes of organelles where they mediate critical cellular processes. Accordingly, mutations in genes encoding TA proteins have been identified in a number of severe inherited disorders. Despite the importance of correctly targeting a TA protein to its appropriate membrane, the mechanisms and signals involved are not fully understood. In this study, we identify additional peroxisomal TA proteins, discover more proteins that are present on multiple organelles, and reveal that a combination of TMD hydrophobicity and tail charge determines targeting to distinct organelle locations in mammals. Specifically, an increase in tail charge can override a hydrophobic TMD signal and re-direct a protein from the ER to peroxisomes or mitochondria and vice versa. We show that subtle changes in those parameters can shift TA proteins between organelles, explaining why peroxisomes and mitochondria have many of the same TA proteins. This enabled us to associate characteristic physicochemical parameters in TA proteins with particular organelle groups. Using this classification allowed successful prediction of the location of uncharacterized TA proteins for the first time. © 2017. Published by The Company of Biologists Ltd.
dc.publisherCompany of Biologists Ltd
dc.sourceUnpaywall 20200831
dc.subjectcell membrane protein
dc.subjecttail anchored protein
dc.subjectunclassified drug
dc.subjectmembrane protein
dc.subjectanimal cell
dc.subjectanimal tissue
dc.subjectArticle
dc.subjectcell fractionation
dc.subjectcell membrane
dc.subjectcell organelle
dc.subjectcontrolled study
dc.subjectendoplasmic reticulum
dc.subjecthuman
dc.subjecthuman cell
dc.subjecthydrophobicity
dc.subjectmammal cell
dc.subjectmitochondrion
dc.subjectnonhuman
dc.subjectperoxisome
dc.subjectprediction
dc.subjectpriority journal
dc.subjectprotein domain
dc.subjectprotein targeting
dc.subjectrat
dc.subjectanimal
dc.subjectbiological model
dc.subjectcell compartmentalization
dc.subjectchemical phenomena
dc.subjectchemistry
dc.subjectHep-G2 cell line
dc.subjectintracellular membrane
dc.subjectmammal
dc.subjectmetabolism
dc.subjectprotein transport
dc.subjectSaccharomyces cerevisiae
dc.subjectAnimals
dc.subjectCell Compartmentation
dc.subjectEndoplasmic Reticulum
dc.subjectHep G2 Cells
dc.subjectHumans
dc.subjectHydrophobic and Hydrophilic Interactions
dc.subjectIntracellular Membranes
dc.subjectMammals
dc.subjectMembrane Proteins
dc.subjectMitochondria
dc.subjectModels, Biological
dc.subjectPeroxisomes
dc.subjectProtein Transport
dc.subjectSaccharomyces cerevisiae
dc.subjectSubcellular Fractions
dc.typeArticle
dc.contributor.departmentDEPT OF BIOLOGICAL SCIENCES
dc.description.doi10.1242/jcs.200204
dc.description.sourcetitleJournal of Cell Science
dc.description.volume130
dc.description.issue9
dc.description.page1675-1687
dc.published.statePublished
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