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Predicting the targeting of tail-anchored proteins to subcellular compartments in mammalian cells

Standard

Predicting the targeting of tail-anchored proteins to subcellular compartments in mammalian cells. / Costello, Joseph L; Castro, Inês G; Camões, Fátima; Schrader, Tina A; McNeall, Doug; Yang, Jing; Giannopoulou, Evdokia-Anastasia; Gomes, Sílvia; Pogenberg, Vivian; Bonekamp, Nina A; Ribeiro, Daniela; Wilmanns, Matthias; Jedd, Gregory; Islinger, Markus; Schrader, Michael.

in: J CELL SCI, Jahrgang 130, Nr. 9, 01.05.2017, S. 1675-1687.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Costello, JL, Castro, IG, Camões, F, Schrader, TA, McNeall, D, Yang, J, Giannopoulou, E-A, Gomes, S, Pogenberg, V, Bonekamp, NA, Ribeiro, D, Wilmanns, M, Jedd, G, Islinger, M & Schrader, M 2017, 'Predicting the targeting of tail-anchored proteins to subcellular compartments in mammalian cells', J CELL SCI, Jg. 130, Nr. 9, S. 1675-1687. https://doi.org/10.1242/jcs.200204

APA

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. J CELL SCI, 130(9), 1675-1687. https://doi.org/10.1242/jcs.200204

Vancouver

Costello JL, Castro IG, Camões F, Schrader TA, McNeall D, Yang J et al. Predicting the targeting of tail-anchored proteins to subcellular compartments in mammalian cells. J CELL SCI. 2017 Mai 1;130(9):1675-1687. https://doi.org/10.1242/jcs.200204

Bibtex

@article{03fab93e64cd47939593d322bc1c3617,
title = "Predicting the targeting of tail-anchored proteins to subcellular compartments in mammalian cells",
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.",
keywords = "Animals, Cell Compartmentation, Endoplasmic Reticulum/metabolism, Hep G2 Cells, Humans, Hydrophobic and Hydrophilic Interactions, Intracellular Membranes/metabolism, Mammals/metabolism, Membrane Proteins/chemistry, Mitochondria/metabolism, Models, Biological, Peroxisomes/metabolism, Protein Transport, Saccharomyces cerevisiae/metabolism, Subcellular Fractions/metabolism",
author = "Costello, {Joseph L} and Castro, {In{\^e}s G} and F{\'a}tima Cam{\~o}es and Schrader, {Tina A} and Doug McNeall and Jing Yang and Evdokia-Anastasia Giannopoulou and S{\'i}lvia Gomes and Vivian Pogenberg and Bonekamp, {Nina A} and Daniela Ribeiro and Matthias Wilmanns and Gregory Jedd and Markus Islinger and Michael Schrader",
note = "{\textcopyright} 2017. Published by The Company of Biologists Ltd.",
year = "2017",
month = may,
day = "1",
doi = "10.1242/jcs.200204",
language = "English",
volume = "130",
pages = "1675--1687",
journal = "J CELL SCI",
issn = "0021-9533",
publisher = "Company of Biologists Ltd",
number = "9",

}

RIS

TY - JOUR

T1 - Predicting the targeting of tail-anchored proteins to subcellular compartments in mammalian cells

AU - Costello, Joseph L

AU - Castro, Inês G

AU - Camões, Fátima

AU - Schrader, Tina A

AU - McNeall, Doug

AU - Yang, Jing

AU - Giannopoulou, Evdokia-Anastasia

AU - Gomes, Sílvia

AU - Pogenberg, Vivian

AU - Bonekamp, Nina A

AU - Ribeiro, Daniela

AU - Wilmanns, Matthias

AU - Jedd, Gregory

AU - Islinger, Markus

AU - Schrader, Michael

N1 - © 2017. Published by The Company of Biologists Ltd.

PY - 2017/5/1

Y1 - 2017/5/1

N2 - 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.

AB - 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.

KW - Animals

KW - Cell Compartmentation

KW - Endoplasmic Reticulum/metabolism

KW - Hep G2 Cells

KW - Humans

KW - Hydrophobic and Hydrophilic Interactions

KW - Intracellular Membranes/metabolism

KW - Mammals/metabolism

KW - Membrane Proteins/chemistry

KW - Mitochondria/metabolism

KW - Models, Biological

KW - Peroxisomes/metabolism

KW - Protein Transport

KW - Saccharomyces cerevisiae/metabolism

KW - Subcellular Fractions/metabolism

U2 - 10.1242/jcs.200204

DO - 10.1242/jcs.200204

M3 - SCORING: Journal article

C2 - 28325759

VL - 130

SP - 1675

EP - 1687

JO - J CELL SCI

JF - J CELL SCI

SN - 0021-9533

IS - 9

ER -