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| Item Type: | Article |
|---|---|
| Title: | Signal peptide cleavage of a type I membrane protein, HCMV US11, is dependent on its membrane anchor |
| Creators Name: | Rehm, A., Stern, P., Ploegh, H.L. and Tortorella, D. |
| Abstract: | The human cytomegalovirus (HCMV) US11 polypeptide is a type I membrane glycoprotein that targets major histocompatibility complex (MHC) class I molecules for destruction in a proteasome-dependent manner. Although the US11 signal sequence appears to be a classical N-terminal signal peptide in terms of its sequence and cleavage site, a fraction of newly synthesized US11 molecules retain the signal peptide after the N-linked glycan has been attached and translation of the US11 polypeptide has been completed. Delayed cleavage of the US11 signal peptide is determined by the first four residues, the so-called n-region of the signal peptide. Its replacement with the four N-terminal residues of the H-2K b signal sequence eliminates delayed cleavage. Surprisingly, a second region that affects the rate and extent of signal peptide cleavage is the transmembrane region close to the C-terminus of US11. Deletion of the transmembrane region of US11 (US11-180) significantly delays processing, a delay overcome by replacement with the H-2K b signal sequence. Thus, elements at a considerable distance from the signal sequence affect its cleavage. |
| Keywords: | ER Subdomains, HCMV US11, Posttranslational ER Processing, Signal Sequence Cleavage, Transmembrane Anchor |
| Source: | EMBO Journal |
| ISSN: | 0261-4189 |
| Publisher: | Oxford University Press |
| Volume: | 20 |
| Number: | 7 |
| Page Range: | 1573-1582 |
| Date: | 2 April 2001 |
| Official Publication: | https://doi.org/10.1093/emboj/20.7.1573 |
| PubMed: | View item in PubMed |
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