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SEC18/NSF-independent, protein-sorting pathway from the yeast cortical ER to the plasma membrane

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SEC18/NSF-independent, protein-sorting pathway from the yeast cortical ER to the plasma membrane. / Jüschke, Christoph; Wächter, Andrea; Schwappach, Blanche; Seedorf, Matthias.

In: J CELL BIOL, Vol. 169, No. 4, 23.05.2005, p. 613-22.

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

Harvard

Jüschke, C, Wächter, A, Schwappach, B & Seedorf, M 2005, 'SEC18/NSF-independent, protein-sorting pathway from the yeast cortical ER to the plasma membrane', J CELL BIOL, vol. 169, no. 4, pp. 613-22. https://doi.org/10.1083/jcb.200503033

APA

Jüschke, C., Wächter, A., Schwappach, B., & Seedorf, M. (2005). SEC18/NSF-independent, protein-sorting pathway from the yeast cortical ER to the plasma membrane. J CELL BIOL, 169(4), 613-22. https://doi.org/10.1083/jcb.200503033

Vancouver

Jüschke C, Wächter A, Schwappach B, Seedorf M. SEC18/NSF-independent, protein-sorting pathway from the yeast cortical ER to the plasma membrane. J CELL BIOL. 2005 May 23;169(4):613-22. https://doi.org/10.1083/jcb.200503033

Bibtex

@article{b9522e3b76184226a419037e9ab2330f,
title = "SEC18/NSF-independent, protein-sorting pathway from the yeast cortical ER to the plasma membrane",
abstract = "Classic studies of temperature-sensitive secretory (sec) mutants have demonstrated that secreted and plasma membrane proteins follow a common SEC pathway via the endoplasmic reticulum (ER), Golgi apparatus, and secretory vesicles to the cell periphery. The yeast protein Ist2p, which is synthesized from a localized mRNA, travels from the ER to the plasma membrane via a novel route that operates independently of the formation of coat protein complex II-coated vesicles. In this study, we show that the COOH-terminal domain of Ist2p is necessary and sufficient to mediate SEC18-independent sorting when it is positioned at the COOH terminus of different integral membrane proteins and exposed to the cytoplasm. This domain functions as a dominant plasma membrane localization determinant that overrides other protein sorting signals. Based on these observations, we suggest a local synthesis of Ist2p at cortical ER sites, from where the protein is sorted by a novel mechanism to the plasma membrane.",
keywords = "Adenosine Triphosphatases/metabolism, Carrier Proteins/metabolism, Cell Membrane/metabolism, Endoplasmic Reticulum/metabolism, Membrane Proteins/metabolism, Protein Structure, Tertiary/physiology, Protein Transport/physiology, Saccharomyces cerevisiae/genetics, Saccharomyces cerevisiae Proteins/metabolism, Signal Transduction/physiology, Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins, Transport Vesicles/metabolism, Vesicular Transport Proteins/metabolism",
author = "Christoph J{\"u}schke and Andrea W{\"a}chter and Blanche Schwappach and Matthias Seedorf",
year = "2005",
month = may,
day = "23",
doi = "10.1083/jcb.200503033",
language = "English",
volume = "169",
pages = "613--22",
journal = "J CELL BIOL",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "4",

}

RIS

TY - JOUR

T1 - SEC18/NSF-independent, protein-sorting pathway from the yeast cortical ER to the plasma membrane

AU - Jüschke, Christoph

AU - Wächter, Andrea

AU - Schwappach, Blanche

AU - Seedorf, Matthias

PY - 2005/5/23

Y1 - 2005/5/23

N2 - Classic studies of temperature-sensitive secretory (sec) mutants have demonstrated that secreted and plasma membrane proteins follow a common SEC pathway via the endoplasmic reticulum (ER), Golgi apparatus, and secretory vesicles to the cell periphery. The yeast protein Ist2p, which is synthesized from a localized mRNA, travels from the ER to the plasma membrane via a novel route that operates independently of the formation of coat protein complex II-coated vesicles. In this study, we show that the COOH-terminal domain of Ist2p is necessary and sufficient to mediate SEC18-independent sorting when it is positioned at the COOH terminus of different integral membrane proteins and exposed to the cytoplasm. This domain functions as a dominant plasma membrane localization determinant that overrides other protein sorting signals. Based on these observations, we suggest a local synthesis of Ist2p at cortical ER sites, from where the protein is sorted by a novel mechanism to the plasma membrane.

AB - Classic studies of temperature-sensitive secretory (sec) mutants have demonstrated that secreted and plasma membrane proteins follow a common SEC pathway via the endoplasmic reticulum (ER), Golgi apparatus, and secretory vesicles to the cell periphery. The yeast protein Ist2p, which is synthesized from a localized mRNA, travels from the ER to the plasma membrane via a novel route that operates independently of the formation of coat protein complex II-coated vesicles. In this study, we show that the COOH-terminal domain of Ist2p is necessary and sufficient to mediate SEC18-independent sorting when it is positioned at the COOH terminus of different integral membrane proteins and exposed to the cytoplasm. This domain functions as a dominant plasma membrane localization determinant that overrides other protein sorting signals. Based on these observations, we suggest a local synthesis of Ist2p at cortical ER sites, from where the protein is sorted by a novel mechanism to the plasma membrane.

KW - Adenosine Triphosphatases/metabolism

KW - Carrier Proteins/metabolism

KW - Cell Membrane/metabolism

KW - Endoplasmic Reticulum/metabolism

KW - Membrane Proteins/metabolism

KW - Protein Structure, Tertiary/physiology

KW - Protein Transport/physiology

KW - Saccharomyces cerevisiae/genetics

KW - Saccharomyces cerevisiae Proteins/metabolism

KW - Signal Transduction/physiology

KW - Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins

KW - Transport Vesicles/metabolism

KW - Vesicular Transport Proteins/metabolism

U2 - 10.1083/jcb.200503033

DO - 10.1083/jcb.200503033

M3 - SCORING: Journal article

C2 - 15911878

VL - 169

SP - 613

EP - 622

JO - J CELL BIOL

JF - J CELL BIOL

SN - 0021-9525

IS - 4

ER -