NDLI: Sequence, linkage to H2-K, and function of mouse tapasin in MHC class I assembly

Content Provider	Springer Nature Link
Author	Grandea III., A. G. Comber, Paul G. Wenderfer, Scott E. Schoenhals, Gary Früh, Klaus Monaco, John J. Spies, T.
Copyright Year	1998
Abstract	Assembly of major histocompatibility complex (MHC) class I molecules in human cells is dependent on the accessory protein tapasin, which mediates their interaction with the transporters associated with antigen processing (TAP) and thereby ensures efficient peptide binding. Analysis of a mouse tapasin complementary DNA defined a conserved polypeptide sharing sequences diagnostic of a transmembrane protein related to the immunoglobulin superfamily, and an endoplasmic reticulum retention motif. The mouse tapasin gene was mapped about 70 kilobases from H2-K at the centromeric end of the mouse MHC. Expression of mouse tapasin in a tapasin-deficient human mutant cell line restored the normal assembly and expression of class I alleles. Thus, tapasin is a structurally and functionally conserved component of the MHC class I antigen processing pathway. Its genetic linkage to the class I and TAP subunit genes in the MHC may be of significance in the coordinate expression and functional coadaptation of the diverse gene products.
Starting Page	260
Ending Page	265
Page Count	6
File Format	PDF
ISSN	00937711
Journal	Immunogenetics
Volume Number	48
Issue Number	4
e-ISSN	14321211
Language	English
Publisher	Springer-Verlag
Publisher Date	1998-08-27
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Content Type	Text
Resource Type	Article
Subject	Genetics Immunology

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