TAPBPR isoforms exhibit altered association with MHC class I. Issue 2 (June 2014)

• Record Type: Journal Article
• Authors: Porter, Keith M.; Hermann, Clemens; Traherne, James A.; Boyle, Louise H.
• Is Part Of: Immunology. Volume 142:Issue 2(2014:Jun.)
• Page Start: 289
• Page End: 299
• Publication Date: 2014-06
• Subjects: Immunology -- Periodicals
• DOI: 10.1111/imm.12253
• Languages: English
• ISSNs: 0019-2805

Abstract

<abstract abstract-type="main" id="imm12253-abs-0001"> <title>Summary</title> <p>The tapasin‐related protein TAPBPR is a novel component of the antigen processing and presentation pathway, which binds to MHC class I coupled with <italic>β</italic>₂‐microglobulin. We describe six alternatively spliced TAPBPR transcripts from the <italic>TAPBPL</italic> gene and investigate three of these at a protein level. TAPBPR transcripts lacking exon 5 result in loss of the membrane proximal IgC domain and loss of ability to bind to MHC class I. Alternative acceptor and donor splice sites in exon 4 of TAPBPR altered the reading frame in the IgV domain and produced a truncated TAPBPR product. An additional exon in the <italic>TAPBPL</italic> gene was identified that encodes extra residues in the cytoplasmic tail of TAPBPR. This longer TAPBPR protein interacted with MHC class I but was attenuated in its ability to down‐regulate surface expression of MHC class I. The abundance of these alternative transcripts in peripheral blood mononuclear cells and dendritic cells suggests an important role of TAPBPR isoforms <italic>in vivo</italic>.</p> </abstract>