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Originally published In Press as doi:10.1074/jbc.M210158200 on December 12, 2002

J. Biol. Chem., Vol. 278, Issue 9, 6664-6672, February 28, 2003
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Protein Unfolding Is Not a Prerequisite for Endoplasmic Reticulum-to-Cytosol Dislocation*

Boaz TiroshDagger , Margo H. Furman, Domenico Tortorella, and Hidde L. Ploegh§

From the Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115

We examined the effects of protein folding on endoplasmic reticulum (ER)-to-cytosol transport (dislocation) by exploiting the well-characterized dihydrofolate reductase (DHFR) domain. DHFR retains the capacity to bind folate analogues in the lumen of microsomes and in the ER of intact cells, upon which it acquires a conformation resistant to proteinase K digestion. Here we show that a Class I major histocompatibility complex heavy chain fused to DHFR is still recognized by the human cytomegalovirus-encoded glycoproteins US2 and US11, resulting in dislocation of the fusion protein from the ER in vitro and in vivo. A folded state of the DHFR domain does not impair dislocation of Class I MHC heavy chains in vitro or in living cells. In fact, a slight acceleration of the dislocation of DHFR heavy chain fusion was observed in vitro in the presence of a folate analogue. These results suggest that one or more of the channels used for dislocation can accommodate polypeptides that contain a tightly folded domain of considerable size. Our data raise the possibility that the Sec61 channel can be modified to accommodate a folded DHFR domain for dislocation, but not for translocation into the ER, or that a channel altogether distinct from Sec61 is used for dislocation.

* This work was supported in part by National Institutes of Health Grant 5R37-AI33456.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Supported by a Dorot Foundation fellowship.

§ To whom correspondence should be addressed: Dept. of Pathology, Harvard Medical School, 200 Longwood Ave. Armenise Bldg., Rm. 137, Boston, MA 02115. Tel.: 617-432-4777; Fax: 617-432-4775; E-mail: hidde_ploegh@hms.harvard.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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