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J. Biol. Chem., Vol. 282, Issue 42, 30680-30690, October 19, 2007

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Peptide-receptive Major Histocompatibility Complex Class I Molecules Cycle between Endoplasmic Reticulum and cis-Golgi in Wild-type Lymphocytes^*

Malgorzata Garstka¹, Britta Borchert¹, Mohammed Al-Balushi¹, PVK Praveen, Nicole Kühl, Irina Majoul^¶, Rainer Duden^¶, and Sebastian Springer²

From the Biochemistry and Cell Biology, School of Engineering and Science, Jacobs University Bremen, 28759 Bremen, Germany, the Department of Microbiology and Immunology, Sultan Qaboos University, Muscat 123, Oman, and the ^¶School of Biological Sciences, Royal Holloway University of London, Egham, Surrey TW20 0EX, United Kingdom

Prior to binding to a high affinity peptide and transporting it to the cell surface, major histocompatibility complex class I molecules are retained inside the cell by retention in the endoplasmic reticulum (ER), recycling through the ER-Golgi intermediate compartment and possibly the cis-Golgi, or both. Using fluorescence microscopy and a novel in vitro COPII (ER-to-ER-Golgi intermediate compartment) vesicle formation assay, we find that in both lymphocytes and fibroblasts that lack the functional transporter associated with antigen presentation, class I molecules exit the ER and reach the cis-Golgi. Intriguingly, in wild-type T1 lymphoma cells, peptide-occupied and peptide-receptive class I molecules are simultaneously exported from ER membranes with similar efficiencies. Our results suggest that binding of high affinity peptide and exit from the ER are not coupled, that the major histocompatibility complex class I quality control compartment extends into the Golgi apparatus under standard conditions, and that peptide loading onto class I molecules may occur in post-ER compartments.

Received for publication, February 27, 2007 , and in revised form, July 9, 2007.

^* This work was supported by Deutsche Forschungsgemeinschaft Grant SP583/2-2 (to S. Sp.) and Wellcome Trust Grant 047578 (to R. D.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement"in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1–S6.

¹ These authors contributed equally to this work.

² To whom correspondence should be addressed. Tel.: 49-421-200-3243; Fax: 49-421-200-3249; E-mail: s.springer{at}jacobs-university.de.

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