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Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum

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Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum. / Jonikas, Martin C; Collins, Sean R; Denic, Vladimir; Oh, Eugene; Quan, Erin M; Schmid, Volker; Weibezahn, Jimena; Schwappach, Blanche; Walter, Peter; Weissman, Jonathan S; Schuldiner, Maya.

In: SCIENCE, Vol. 323, No. 5922, 27.03.2009, p. 1693-7.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Jonikas, MC, Collins, SR, Denic, V, Oh, E, Quan, EM, Schmid, V, Weibezahn, J, Schwappach, B, Walter, P, Weissman, JS & Schuldiner, M 2009, 'Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum', SCIENCE, vol. 323, no. 5922, pp. 1693-7. https://doi.org/10.1126/science.1167983

APA

Jonikas, M. C., Collins, S. R., Denic, V., Oh, E., Quan, E. M., Schmid, V., Weibezahn, J., Schwappach, B., Walter, P., Weissman, J. S., & Schuldiner, M. (2009). Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum. SCIENCE, 323(5922), 1693-7. https://doi.org/10.1126/science.1167983

Vancouver

Jonikas MC, Collins SR, Denic V, Oh E, Quan EM, Schmid V et al. Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum. SCIENCE. 2009 Mar 27;323(5922):1693-7. https://doi.org/10.1126/science.1167983

Bibtex

@article{ff979a2537504e5a95ba670d9cefb8ae,
title = "Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum",
abstract = "Protein folding in the endoplasmic reticulum is a complex process whose malfunction is implicated in disease and aging. By using the cell's endogenous sensor (the unfolded protein response), we identified several hundred yeast genes with roles in endoplasmic reticulum folding and systematically characterized their functional interdependencies by measuring unfolded protein response levels in double mutants. This strategy revealed multiple conserved factors critical for endoplasmic reticulum folding, including an intimate dependence on the later secretory pathway, a previously uncharacterized six-protein transmembrane complex, and a co-chaperone complex that delivers tail-anchored proteins to their membrane insertion machinery. The use of a quantitative reporter in a comprehensive screen followed by systematic analysis of genetic dependencies should be broadly applicable to functional dissection of complex cellular processes from yeast to human.",
keywords = "Endoplasmic Reticulum/metabolism, Epistasis, Genetic, Gene Deletion, Gene Expression Regulation, Fungal, Genes, Fungal, Genes, Reporter, Membrane Proteins/chemistry, Mutation, Phenotype, Protein Folding, Protein Processing, Post-Translational, Protein Structure, Tertiary, Saccharomyces cerevisiae/genetics, Saccharomyces cerevisiae Proteins/chemistry, Secretory Pathway",
author = "Jonikas, {Martin C} and Collins, {Sean R} and Vladimir Denic and Eugene Oh and Quan, {Erin M} and Volker Schmid and Jimena Weibezahn and Blanche Schwappach and Peter Walter and Weissman, {Jonathan S} and Maya Schuldiner",
year = "2009",
month = mar,
day = "27",
doi = "10.1126/science.1167983",
language = "English",
volume = "323",
pages = "1693--7",
journal = "SCIENCE",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "5922",

}

RIS

TY - JOUR

T1 - Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum

AU - Jonikas, Martin C

AU - Collins, Sean R

AU - Denic, Vladimir

AU - Oh, Eugene

AU - Quan, Erin M

AU - Schmid, Volker

AU - Weibezahn, Jimena

AU - Schwappach, Blanche

AU - Walter, Peter

AU - Weissman, Jonathan S

AU - Schuldiner, Maya

PY - 2009/3/27

Y1 - 2009/3/27

N2 - Protein folding in the endoplasmic reticulum is a complex process whose malfunction is implicated in disease and aging. By using the cell's endogenous sensor (the unfolded protein response), we identified several hundred yeast genes with roles in endoplasmic reticulum folding and systematically characterized their functional interdependencies by measuring unfolded protein response levels in double mutants. This strategy revealed multiple conserved factors critical for endoplasmic reticulum folding, including an intimate dependence on the later secretory pathway, a previously uncharacterized six-protein transmembrane complex, and a co-chaperone complex that delivers tail-anchored proteins to their membrane insertion machinery. The use of a quantitative reporter in a comprehensive screen followed by systematic analysis of genetic dependencies should be broadly applicable to functional dissection of complex cellular processes from yeast to human.

AB - Protein folding in the endoplasmic reticulum is a complex process whose malfunction is implicated in disease and aging. By using the cell's endogenous sensor (the unfolded protein response), we identified several hundred yeast genes with roles in endoplasmic reticulum folding and systematically characterized their functional interdependencies by measuring unfolded protein response levels in double mutants. This strategy revealed multiple conserved factors critical for endoplasmic reticulum folding, including an intimate dependence on the later secretory pathway, a previously uncharacterized six-protein transmembrane complex, and a co-chaperone complex that delivers tail-anchored proteins to their membrane insertion machinery. The use of a quantitative reporter in a comprehensive screen followed by systematic analysis of genetic dependencies should be broadly applicable to functional dissection of complex cellular processes from yeast to human.

KW - Endoplasmic Reticulum/metabolism

KW - Epistasis, Genetic

KW - Gene Deletion

KW - Gene Expression Regulation, Fungal

KW - Genes, Fungal

KW - Genes, Reporter

KW - Membrane Proteins/chemistry

KW - Mutation

KW - Phenotype

KW - Protein Folding

KW - Protein Processing, Post-Translational

KW - Protein Structure, Tertiary

KW - Saccharomyces cerevisiae/genetics

KW - Saccharomyces cerevisiae Proteins/chemistry

KW - Secretory Pathway

U2 - 10.1126/science.1167983

DO - 10.1126/science.1167983

M3 - SCORING: Journal article

C2 - 19325107

VL - 323

SP - 1693

EP - 1697

JO - SCIENCE

JF - SCIENCE

SN - 0036-8075

IS - 5922

ER -