Please use this identifier to cite or link to this item: https://doi.org/10.1242/jcs.200204
Title: Predicting the targeting of tail-anchored proteins to subcellular compartments in mammalian cells
Authors: Costello 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.
Keywords: cell membrane protein
tail anchored protein
unclassified drug
membrane protein
animal cell
animal tissue
Article
cell fractionation
cell membrane
cell organelle
controlled study
endoplasmic reticulum
human
human cell
hydrophobicity
mammal cell
mitochondrion
nonhuman
peroxisome
prediction
priority journal
protein domain
protein targeting
rat
animal
biological model
cell compartmentalization
chemical phenomena
chemistry
Hep-G2 cell line
intracellular membrane
mammal
metabolism
protein transport
Saccharomyces cerevisiae
Animals
Cell Compartmentation
Endoplasmic Reticulum
Hep G2 Cells
Humans
Hydrophobic and Hydrophilic Interactions
Intracellular Membranes
Mammals
Membrane Proteins
Mitochondria
Models, Biological
Peroxisomes
Protein Transport
Saccharomyces cerevisiae
Subcellular Fractions
Issue Date: 2017
Publisher: Company of Biologists Ltd
Citation: Costello 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
Abstract: Tail-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.
Source Title: Journal of Cell Science
URI: https://scholarbank.nus.edu.sg/handle/10635/175225
ISSN: 0021-9533
DOI: 10.1242/jcs.200204
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