| First Author | Früh K | Year | 1992 |
| Journal | J Biol Chem | Volume | 267 |
| Issue | 31 | Pages | 22131-40 |
| PubMed ID | 1429565 | Mgi Jnum | J:21811 |
| Mgi Id | MGI:69717 | Doi | 10.1016/s0021-9258(18)41645-6 |
| Citation | Fruh K, et al. (1992) Alternative exon usage and processing of the major histocompatibility complex-encoded proteasome subunits. J Biol Chem 267(31):22131-40 |
| abstractText | The finding that two subunits of the proteasome, LMP2 and LMP7, are encoded in the major histocompatibility complex (MHC) has linked the proteasome which represents a major extralysosomal proteolytic system to the processing of intracellular antigens. Here we describe a second form of the human LMP7 cDNA, LMP7-E2, which has been identified during the characterization of novel genes in the MHC. The analysis of the genome organization of LMP7 revealed that LMP7-E1 and LMP7-E2 arise by alternative exon usage. Using specific antibodies against LMP2 and LMP7, we show that they are co-expressed with class I MHC molecules as well as a putative peptide transporter. The polypeptides encoded by LMP7 and LMP2 undergo proteolytic processing when incorporated into proteasomes, and the LMP7 precursor is derived mainly from LMP7-E2. Furthermore, our data suggest that LMP7 and LMP2 are mutually dependent for their incorporation into the proteasomal complex. |
