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Amyloid Precursor-Like Protein 2 Increases the Endocytosis, Instability, and Turnover of the H2-K^d MHC Class I Molecule¹

Amit Tuli^*,, Mahak Sharma^*, Mary M. McIlhaney, James E. Talmadge, Naava Naslavsky^*, Steve Caplan^* and Joyce C. Solheim^2,*,,

^* Department of Biochemistry and Molecular Biology, Eppley Institute for Research in Cancer and Allied Diseases, and Department of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, NE 68198

The defense against the invasion of viruses and tumors relies on the presentation of viral and tumor-derived peptides to CTL by cell surface MHC class I molecules. Previously, we showed that the ubiquitously expressed protein amyloid precursor-like protein 2 (APLP2) associates with the folded form of the MHC class I molecule K^d. In the current study, APLP2 was found to associate with folded K^d molecules following their endocytosis and to increase the amount of endocytosed K^d. In addition, increased expression of APLP2 was shown to decrease K^d surface expression and thermostability. Correspondingly, K^d thermostability and surface expression were increased by down-regulation of APLP2 expression. Overall, these data suggest that APLP2 modulates the stability and endocytosis of K^d molecules.

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.

¹ This work was supported by National Institutes of Health Grant GM57428 (to J.C.S.) and GM74876 (to S.C.), the Nebraska Research Initiative Program in Translational Biotechnology Research (to J.E.T. and J.C.S.), University of Nebraska Medical Center Graduate Studies Fellowships (to A.T. and M.S.), and a Nebraska Center for Cellular Signaling Fellowship (to M.S.). Core facilities at the University of Nebraska Medical Center receive support from the National Institutes of Health Cancer Center Support Grant P30 CA036727.

² Address correspondence and reprint requests to Dr. Joyce C. Solheim, Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, 986805 Nebraska Medical Center, Omaha, NE 68198-6805. E-mail address: jsolheim{at}unmc.edu

³ Abbreviations used in this paper: β₂m, β 2-microglobulin; ER, endoplasmic reticulum; APLP2, amyloid precursor-like protein 2; APP, amyloid precursor protein; CHAPS, 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate; Endo, endoglycosidase; EHD1, Eps15 homology domain-containing protein.