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The GET complex mediates insertion of tail-anchored proteins into the ER membrane

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The GET complex mediates insertion of tail-anchored proteins into the ER membrane. / Schuldiner, Maya; Metz, Jutta; Schmid, Volker; Denic, Vladimir; Rakwalska, Magdalena; Schmitt, Hans Dieter; Schwappach, Blanche; Weissman, Jonathan S.

In: CELL, Vol. 134, No. 4, 22.08.2008, p. 634-45.

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

Harvard

Schuldiner, M, Metz, J, Schmid, V, Denic, V, Rakwalska, M, Schmitt, HD, Schwappach, B & Weissman, JS 2008, 'The GET complex mediates insertion of tail-anchored proteins into the ER membrane', CELL, vol. 134, no. 4, pp. 634-45. https://doi.org/10.1016/j.cell.2008.06.025

APA

Schuldiner, M., Metz, J., Schmid, V., Denic, V., Rakwalska, M., Schmitt, H. D., Schwappach, B., & Weissman, J. S. (2008). The GET complex mediates insertion of tail-anchored proteins into the ER membrane. CELL, 134(4), 634-45. https://doi.org/10.1016/j.cell.2008.06.025

Vancouver

Schuldiner M, Metz J, Schmid V, Denic V, Rakwalska M, Schmitt HD et al. The GET complex mediates insertion of tail-anchored proteins into the ER membrane. CELL. 2008 Aug 22;134(4):634-45. https://doi.org/10.1016/j.cell.2008.06.025

Bibtex

@article{f23c6703242d4cd3b5946e65f3f58208,
title = "The GET complex mediates insertion of tail-anchored proteins into the ER membrane",
abstract = "Tail-anchored (TA) proteins, defined by the presence of a single C-terminal transmembrane domain (TMD), play critical roles throughout the secretory pathway and in mitochondria, yet the machinery responsible for their proper membrane insertion remains poorly characterized. Here we show that Get3, the yeast homolog of the TA-interacting factor Asna1/Trc40, specifically recognizes TMDs of TA proteins destined for the secretory pathway. Get3 recognition represents a key decision step, whose loss can lead to misinsertion of TA proteins into mitochondria. Get3-TA protein complexes are recruited for endoplasmic reticulum (ER) membrane insertion by the Get1/Get2 receptor. In vivo, the absence of Get1/Get2 leads to cytosolic aggregation of Get3-TA complexes and broad defects in TA protein biogenesis. In vitro reconstitution demonstrates that the Get proteins directly mediate insertion of newly synthesized TA proteins into ER membranes. Thus, the GET complex represents a critical mechanism for ensuring efficient and accurate targeting of TA proteins.",
keywords = "Adaptor Proteins, Vesicular Transport, Adenosine Triphosphatases, Endoplasmic Reticulum/metabolism, Guanine Nucleotide Exchange Factors/metabolism, Membrane Proteins/metabolism, Protein Structure, Tertiary, Saccharomyces cerevisiae/cytology, Saccharomyces cerevisiae Proteins/metabolism",
author = "Maya Schuldiner and Jutta Metz and Volker Schmid and Vladimir Denic and Magdalena Rakwalska and Schmitt, {Hans Dieter} and Blanche Schwappach and Weissman, {Jonathan S}",
year = "2008",
month = aug,
day = "22",
doi = "10.1016/j.cell.2008.06.025",
language = "English",
volume = "134",
pages = "634--45",
journal = "CELL",
issn = "0092-8674",
publisher = "Cell Press",
number = "4",

}

RIS

TY - JOUR

T1 - The GET complex mediates insertion of tail-anchored proteins into the ER membrane

AU - Schuldiner, Maya

AU - Metz, Jutta

AU - Schmid, Volker

AU - Denic, Vladimir

AU - Rakwalska, Magdalena

AU - Schmitt, Hans Dieter

AU - Schwappach, Blanche

AU - Weissman, Jonathan S

PY - 2008/8/22

Y1 - 2008/8/22

N2 - Tail-anchored (TA) proteins, defined by the presence of a single C-terminal transmembrane domain (TMD), play critical roles throughout the secretory pathway and in mitochondria, yet the machinery responsible for their proper membrane insertion remains poorly characterized. Here we show that Get3, the yeast homolog of the TA-interacting factor Asna1/Trc40, specifically recognizes TMDs of TA proteins destined for the secretory pathway. Get3 recognition represents a key decision step, whose loss can lead to misinsertion of TA proteins into mitochondria. Get3-TA protein complexes are recruited for endoplasmic reticulum (ER) membrane insertion by the Get1/Get2 receptor. In vivo, the absence of Get1/Get2 leads to cytosolic aggregation of Get3-TA complexes and broad defects in TA protein biogenesis. In vitro reconstitution demonstrates that the Get proteins directly mediate insertion of newly synthesized TA proteins into ER membranes. Thus, the GET complex represents a critical mechanism for ensuring efficient and accurate targeting of TA proteins.

AB - Tail-anchored (TA) proteins, defined by the presence of a single C-terminal transmembrane domain (TMD), play critical roles throughout the secretory pathway and in mitochondria, yet the machinery responsible for their proper membrane insertion remains poorly characterized. Here we show that Get3, the yeast homolog of the TA-interacting factor Asna1/Trc40, specifically recognizes TMDs of TA proteins destined for the secretory pathway. Get3 recognition represents a key decision step, whose loss can lead to misinsertion of TA proteins into mitochondria. Get3-TA protein complexes are recruited for endoplasmic reticulum (ER) membrane insertion by the Get1/Get2 receptor. In vivo, the absence of Get1/Get2 leads to cytosolic aggregation of Get3-TA complexes and broad defects in TA protein biogenesis. In vitro reconstitution demonstrates that the Get proteins directly mediate insertion of newly synthesized TA proteins into ER membranes. Thus, the GET complex represents a critical mechanism for ensuring efficient and accurate targeting of TA proteins.

KW - Adaptor Proteins, Vesicular Transport

KW - Adenosine Triphosphatases

KW - Endoplasmic Reticulum/metabolism

KW - Guanine Nucleotide Exchange Factors/metabolism

KW - Membrane Proteins/metabolism

KW - Protein Structure, Tertiary

KW - Saccharomyces cerevisiae/cytology

KW - Saccharomyces cerevisiae Proteins/metabolism

U2 - 10.1016/j.cell.2008.06.025

DO - 10.1016/j.cell.2008.06.025

M3 - SCORING: Journal article

C2 - 18724936

VL - 134

SP - 634

EP - 645

JO - CELL

JF - CELL

SN - 0092-8674

IS - 4

ER -