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J Biol Chem, Vol. 274, Issue 13, 8649-8654, March 26, 1999
From Tumor Immunology, Lund University, Box 7031, S-22007 Lund,
Sweden
Major histocompatibility complex (MHC) class I
molecules present antigenic peptides to CD8 T cells. The peptides are
generated in the cytosol, then translocated across the membrane of the
endoplasmic reticulum by the transporter associated with antigen
processing (TAP). TAP is a trimeric complex consisting of TAP1, TAP2,
and tapasin (TAP-A) as indicated for human cells by reciprocal
coprecipitation with anti-TAP1/2 and anti-tapasin antibodies,
respectively. TAP1 and TAP2 are required for the peptide transport.
Tapasin is involved in the association of class I with TAP and in the
assembly of class I with peptide. The mechanisms of tapasin function
are still unknown. Moreover, there has been no evidence for a murine
tapasin analogue, which has led to the suggestion that murine MHC class I binds directly to TAP1/2. In this study, we have cloned the mouse
analogue of tapasin. The predicted amino acid sequence showed 78%
identity to human tapasin with identical consensus sequences of signal
peptide, N-linked glycosylation site, transmembrane domain
and double lysine motif. However, there was less homology (47%) found
at the predicted cytosolic domain, and in addition, mouse tapasin is 14 amino acids longer than the human analogue at the C terminus. This part
of the molecule may determine the species specificity for interaction
with MHC class I or TAP1/2. Like human tapasin, mouse tapasin binds
both to TAP1/2 and MHC class I. In TAP2-mutated RMA-S cells, both TAP1
and MHC class I were coprecipitated by anti-tapasin antiserum
indicative of association of tapasin with TAP1 but not TAP2. With
crosslinker-modified peptides and purified microsomes, anti-tapasin
coprecipitated both peptide-bound MHC class I and TAP1/2. In contrast,
anti-calreticulin only coprecipitated peptide-free MHC class I
molecules. This difference in association with peptide-loaded class I
suggests that tapasin functions later than calreticulin during MHC
class I assembly, and controls peptide loading onto MHC class I
molecules in the endoplasmic reticulum.
Peptide-bound Major Histocompatibility Complex Class I Molecules
Associate with Tapasin before Dissociation from Transporter Associated
with Antigen Processing
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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