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A more recent version of this article appeared on March 1, 2004
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Submitted on October 27, 2003
Revised on December 2, 2003
Accepted on December 2, 2003
1 Molecular Membrane Biology Laboratory, RIKEN Discovery Research Institute, Wako, Saitama 351-0198, Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, NJ 08854, U.S.A.
2 Molecular Membrane Biology Laboratory, RIKEN Discovery Research Institute, Wako, Saitama 351-0198
3 Molecular Membrane Biology Laboratory, RIKEN Discovery Research Institute, Wako, Saitama 351-0198, and Department of Biological Sciences, Graduate School of Science, University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-0033, Japan
* Corresponding author. E-mail address: nakano{at}postman.riken.go.jp.
Endoplasmic reticulum (ER) quality control is a conserved process by which misfolded or unassembled proteins are selectively retained in the ER. Failure in oligomerization of multisubunit membrane proteins is one of the events that trigger ER quality control. The transmembrane domains (TMDs) of unassembled subunits are determinants of ER retention in many cases, although the mechanism of the TMD-mediated sorting of unassembled subunits remains elusive. We studied a yeast iron transporter complex on the cell surface as a new model system for ER quality control. When Fet3p, a transmembrane subunit, is not assembled with the other membrane subunit, Ftr1p, unassembled Fet3p is exclusively localized to the ER at steady state. The TMD of Fet3p contains a determinant for this process. However, pulse-chase analysis and in vitro budding assays indicate that unassembled Fet3p rapidly escapes from the ER. Furthermore, Rer1p, a retrieval receptor for ER-resident membrane proteins in the Golgi, is responsible for the TMD-dependent ER retrieval of unassembled Fet3p. These findings provide clear evidence that the ER quality control of unassembled membrane proteins can be achieved by retrieval from the Golgi, and that Rer1p serves as a specific sorting receptor in this process.
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