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, Jahrgang 169, Nr. 4, 23.05.2005, S. 613-22.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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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 -