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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
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.
Morris ,
Jason L.
Petersen ,
Shanna E.
Vargas §,
Heth R.
Turnquist §,
Mary M.
McIlhaney ,
Sam D.
Sanderson¶,
Joseph T.
Bruder ,
Yik Y. L.
Yu**,
Hans-Gerhard
Burgert , and
Joyce C.
Solheim §§§¶¶
From the 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
 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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