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Published 23 May 2005. doi:10.1083/jcb.200503033
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 169, Number 4, 613-622
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Article

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

Christoph Jüschke, Andrea Wächter, Blanche Schwappach, and Matthias Seedorf

Center of Molecular Biology, University of Heidelberg, D-69120 Heidelberg, Germany

Correspondence to Matthias Seedorf: m.seedorf{at}zmbh.uni-heidelberg.de

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.

Abbreviations used in this paper: COP, coat protein complex; Hxt, hexose transporter; PC, protein C; sec, secretory; TM, transmembrane; UTR, untranslated region.


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