TAPBPR isoforms exhibit altered association with MHC class I.

ABSTRACT: The tapasin-related protein TAPBPR is a novel component of the antigen processing and presentation pathway, which binds to MHC class I coupled with β2-microglobulin. We describe six alternatively spliced TAPBPR transcripts from the TAPBPL 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 TAPBPL 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 surfa

SUBMITTER: Porter KM 

PROVIDER: S-EPMC4008236 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature