Abstract
Latent membrane protein 2A (LMP2A) of latent Epstein-Barr virus (EBV) specifically associates with HECT domain-containing Nedd4-family ubiquitin-protein ligases (E3s). Here we demonstrate that LMP2A is specifically ubiquitinated by the HECT domains of AIP4 and WWP2. Deletion and site-specific mutation of LMP2A indicates that LMP2A is ubiquitinated at its amino-terminus and is not ubiquitinated on lysine residues. LMP2A and LMP1, also encoded by EBV, are two of only four proteins that have been identified that are ubiquitinated at the amino-terminus, indicating that EBV may specifically target and utilize this host cell protein modification.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 153-159 |
| Number of pages | 7 |
| Journal | Virology |
| Volume | 300 |
| Issue number | 1 |
| DOIs | |
| State | Published - 2002 |
Funding
The HA-tagged uibiquitin (Ub-HA) expression plasmid was provided by Dr. D. Bohmann. R.L. is supported by Public Health Service Grants CA62234 and CA73507 from the National Cancer Institute and DE13127 from the National Institute of Dental and Craniofacial Research. R.L. is a Stohlman Scholar of the Leukemia and Lymphoma Society of America. M.I. is a special fellow of the Leukemia and Lymphoma Society of America.
ASJC Scopus subject areas
- Virology