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A more recent version of this article appeared on July 1, 2003
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Submitted on February 26, 2003
Revised on March 23, 2003
Accepted on March 24, 2003
1 Molecular Membrane Biology Laboratory, RIKEN; and PRESTO, Japan Science and Technology Corporation, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan
2 Molecular Membrane Biology Laboratory, RIKEN
* Corresponding author. E-mail address: kensato{at}postman.riken.go.jp.
Secretory proteins are transported from the endoplasmic reticulum (ER) to the Golgi complex in vesicles coated with coat protein complex II (COPII). The incorporation of certain transport molecules (cargo) into the COPII vesicles is thought to be mediated by cargo receptors. Here we show that Emp47p, a type-I membrane protein, is specifically required for the transport of an integral membrane protein, Emp46p, from the ER. Exit of Emp46p from the ER was saturable and dependent on the expression level of Emp47p. Emp46p binding to Emp47p occurs in the ER through the coiled-coil region in the luminal domains of both Emp47p and Emp46p, and dissociation occurs in the Golgi. Further, this coiled-coil region is also required for Emp47p to form an oligomeric complex of itself in the ER, which is essential for exit of Emp47p from the ER. Our results suggest that Emp47p is a receptor protein for Emp46p that allows for the selective transport of this protein, and this event involves receptor oligomerization.
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