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Originally published In Press as doi:10.1074/jbc.M208203200 on December 27, 2002

J. Biol. Chem., Vol. 278, Issue 15, 12618-12623, April 11, 2003
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The Amyloid Precursor-like Protein 2 and the Adenoviral E3/19K Protein Both Bind to a Conformational Site on H-2Kd and Regulate H-2Kd Expression*

Chantey R. MorrisDagger , Jason L. PetersenDagger , Shanna E. VargasDagger §, Heth R. TurnquistDagger §, Mary M. McIlhaneyDagger , Sam D. Sanderson, Joseph T. Bruder||, Yik Y. L. Yu**, Hans-Gerhard BurgertDagger Dagger , and Joyce C. SolheimDagger §§§¶¶

From the Dagger  Eppley Institute for Research in Cancer and Allied Diseases, the Departments of § Pathology and Microbiology and §§ Biochemistry and Molecular Biology, and the  School of Allied Health Professions, University of Nebraska Medical Center, Omaha, Nebraska 68198, || GenVec, Gaithersburg, Maryland 20878, ** NCI, National Institutes of Health, Bethesda, Maryland 20892, and the Dagger Dagger  Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, United Kingdom

A protein of unknown physiological function, called amyloid precursor-like protein 2 (APLP2), forms an association with the murine class I molecule Kd that is up-regulated by the presence of the adenoviral protein E3/19K. We have extended these findings to show that APLP2 and E3/19K associate preferentially with folded Kd and not with the open form. APLP2 was detectable at the cell surface, but its surface expression was not up-regulated by the concurrent expression of Kd. Experimental down-regulation of APLP2 expression caused a consistent increase in the surface expression of Kd, indicating that APLP2 normally reduces Kd surface expression. These data suggest a role for APLP2 in controlling the maturation of major histocompatibility complex class I molecules.


* This work was supported by Deutsche Forschungsgemeinschaft Grant Bu 642/1 (to H.-G. B.), National Institutes of Health Grant GM57428 (to J. C. S.), and National Institutes of Health Training Grant T32 CA09476 and University of Nebraska Medical Center Graduate Studies Fellowships (to J. L. P., S. E. V., and H. R. T.).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.

¶¶ To whom correspondence should be addressed: Eppley Inst. for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, 986805 Nebraska Medical Center, Omaha, NE 68198-6805. Tel.: 402-559-4539; Fax: 402-559-4651; E-mail: jsolheim@unmc.edu.


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