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The SND proteins constitute an alternative targeting route to the endoplasmic reticulum

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The SND proteins constitute an alternative targeting route to the endoplasmic reticulum. / Aviram, Naama; Ast, Tslil; Costa, Elizabeth A; Arakel, Eric C; Chuartzman, Silvia G; Jan, Calvin H; Haßdenteufel, Sarah; Dudek, Johanna; Jung, Martin; Schorr, Stefan; Zimmermann, Richard; Schwappach, Blanche; Weissman, Jonathan S; Schuldiner, Maya.

in: NATURE, Jahrgang 540, Nr. 7631, 30.11.2016, S. 134-138.

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

Harvard

Aviram, N, Ast, T, Costa, EA, Arakel, EC, Chuartzman, SG, Jan, CH, Haßdenteufel, S, Dudek, J, Jung, M, Schorr, S, Zimmermann, R, Schwappach, B, Weissman, JS & Schuldiner, M 2016, 'The SND proteins constitute an alternative targeting route to the endoplasmic reticulum', NATURE, Jg. 540, Nr. 7631, S. 134-138. https://doi.org/10.1038/nature20169

APA

Aviram, N., Ast, T., Costa, E. A., Arakel, E. C., Chuartzman, S. G., Jan, C. H., Haßdenteufel, S., Dudek, J., Jung, M., Schorr, S., Zimmermann, R., Schwappach, B., Weissman, J. S., & Schuldiner, M. (2016). The SND proteins constitute an alternative targeting route to the endoplasmic reticulum. NATURE, 540(7631), 134-138. https://doi.org/10.1038/nature20169

Vancouver

Aviram N, Ast T, Costa EA, Arakel EC, Chuartzman SG, Jan CH et al. The SND proteins constitute an alternative targeting route to the endoplasmic reticulum. NATURE. 2016 Nov 30;540(7631):134-138. https://doi.org/10.1038/nature20169

Bibtex

@article{d3614372ac9e4db3ae606937165fabad,
title = "The SND proteins constitute an alternative targeting route to the endoplasmic reticulum",
abstract = "In eukaryotes, up to one-third of cellular proteins are targeted to the endoplasmic reticulum, where they undergo folding, processing, sorting and trafficking to subsequent endomembrane compartments. Targeting to the endoplasmic reticulum has been shown to occur co-translationally by the signal recognition particle (SRP) pathway or post-translationally by the mammalian transmembrane recognition complex of 40 kDa (TRC40) and homologous yeast guided entry of tail-anchored proteins (GET) pathways. Despite the range of proteins that can be catered for by these two pathways, many proteins are still known to be independent of both SRP and GET, so there seems to be a critical need for an additional dedicated pathway for endoplasmic reticulum relay. We set out to uncover additional targeting proteins using unbiased high-content screening approaches. To this end, we performed a systematic visual screen using the yeast Saccharomyces cerevisiae, and uncovered three uncharacterized proteins whose loss affected targeting. We suggest that these proteins work together and demonstrate that they function in parallel with SRP and GET to target a broad range of substrates to the endoplasmic reticulum. The three proteins, which we name Snd1, Snd2 and Snd3 (for SRP-independent targeting), can synthetically compensate for the loss of both the SRP and GET pathways, and act as a backup targeting system. This explains why it has previously been difficult to demonstrate complete loss of targeting for some substrates. Our discovery thus puts in place an essential piece of the endoplasmic reticulum targeting puzzle, highlighting how the targeting apparatus of the eukaryotic cell is robust, interlinked and flexible.",
keywords = "Endoplasmic Reticulum/metabolism, HEK293 Cells, Humans, Membrane Proteins/metabolism, Phosphate Transport Proteins/metabolism, Protein Domains, Protein Sorting Signals, Protein Transport, Ribosomal Proteins/metabolism, Saccharomyces cerevisiae/cytology, Saccharomyces cerevisiae Proteins/metabolism, Signal Recognition Particle/metabolism",
author = "Naama Aviram and Tslil Ast and Costa, {Elizabeth A} and Arakel, {Eric C} and Chuartzman, {Silvia G} and Jan, {Calvin H} and Sarah Ha{\ss}denteufel and Johanna Dudek and Martin Jung and Stefan Schorr and Richard Zimmermann and Blanche Schwappach and Weissman, {Jonathan S} and Maya Schuldiner",
year = "2016",
month = nov,
day = "30",
doi = "10.1038/nature20169",
language = "English",
volume = "540",
pages = "134--138",
journal = "NATURE",
issn = "0028-0836",
publisher = "NATURE PUBLISHING GROUP",
number = "7631",

}

RIS

TY - JOUR

T1 - The SND proteins constitute an alternative targeting route to the endoplasmic reticulum

AU - Aviram, Naama

AU - Ast, Tslil

AU - Costa, Elizabeth A

AU - Arakel, Eric C

AU - Chuartzman, Silvia G

AU - Jan, Calvin H

AU - Haßdenteufel, Sarah

AU - Dudek, Johanna

AU - Jung, Martin

AU - Schorr, Stefan

AU - Zimmermann, Richard

AU - Schwappach, Blanche

AU - Weissman, Jonathan S

AU - Schuldiner, Maya

PY - 2016/11/30

Y1 - 2016/11/30

N2 - In eukaryotes, up to one-third of cellular proteins are targeted to the endoplasmic reticulum, where they undergo folding, processing, sorting and trafficking to subsequent endomembrane compartments. Targeting to the endoplasmic reticulum has been shown to occur co-translationally by the signal recognition particle (SRP) pathway or post-translationally by the mammalian transmembrane recognition complex of 40 kDa (TRC40) and homologous yeast guided entry of tail-anchored proteins (GET) pathways. Despite the range of proteins that can be catered for by these two pathways, many proteins are still known to be independent of both SRP and GET, so there seems to be a critical need for an additional dedicated pathway for endoplasmic reticulum relay. We set out to uncover additional targeting proteins using unbiased high-content screening approaches. To this end, we performed a systematic visual screen using the yeast Saccharomyces cerevisiae, and uncovered three uncharacterized proteins whose loss affected targeting. We suggest that these proteins work together and demonstrate that they function in parallel with SRP and GET to target a broad range of substrates to the endoplasmic reticulum. The three proteins, which we name Snd1, Snd2 and Snd3 (for SRP-independent targeting), can synthetically compensate for the loss of both the SRP and GET pathways, and act as a backup targeting system. This explains why it has previously been difficult to demonstrate complete loss of targeting for some substrates. Our discovery thus puts in place an essential piece of the endoplasmic reticulum targeting puzzle, highlighting how the targeting apparatus of the eukaryotic cell is robust, interlinked and flexible.

AB - In eukaryotes, up to one-third of cellular proteins are targeted to the endoplasmic reticulum, where they undergo folding, processing, sorting and trafficking to subsequent endomembrane compartments. Targeting to the endoplasmic reticulum has been shown to occur co-translationally by the signal recognition particle (SRP) pathway or post-translationally by the mammalian transmembrane recognition complex of 40 kDa (TRC40) and homologous yeast guided entry of tail-anchored proteins (GET) pathways. Despite the range of proteins that can be catered for by these two pathways, many proteins are still known to be independent of both SRP and GET, so there seems to be a critical need for an additional dedicated pathway for endoplasmic reticulum relay. We set out to uncover additional targeting proteins using unbiased high-content screening approaches. To this end, we performed a systematic visual screen using the yeast Saccharomyces cerevisiae, and uncovered three uncharacterized proteins whose loss affected targeting. We suggest that these proteins work together and demonstrate that they function in parallel with SRP and GET to target a broad range of substrates to the endoplasmic reticulum. The three proteins, which we name Snd1, Snd2 and Snd3 (for SRP-independent targeting), can synthetically compensate for the loss of both the SRP and GET pathways, and act as a backup targeting system. This explains why it has previously been difficult to demonstrate complete loss of targeting for some substrates. Our discovery thus puts in place an essential piece of the endoplasmic reticulum targeting puzzle, highlighting how the targeting apparatus of the eukaryotic cell is robust, interlinked and flexible.

KW - Endoplasmic Reticulum/metabolism

KW - HEK293 Cells

KW - Humans

KW - Membrane Proteins/metabolism

KW - Phosphate Transport Proteins/metabolism

KW - Protein Domains

KW - Protein Sorting Signals

KW - Protein Transport

KW - Ribosomal Proteins/metabolism

KW - Saccharomyces cerevisiae/cytology

KW - Saccharomyces cerevisiae Proteins/metabolism

KW - Signal Recognition Particle/metabolism

U2 - 10.1038/nature20169

DO - 10.1038/nature20169

M3 - SCORING: Journal article

C2 - 27905431

VL - 540

SP - 134

EP - 138

JO - NATURE

JF - NATURE

SN - 0028-0836

IS - 7631

ER -