Lysine-independent ubiquitination of Epstein-Barr virus LMP2A.
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.
Ikeda
Masato
M
Department of Microbiology-Immunology, Northwestern University Medical School, Chicago, Illinois 60611, USA.
Ikeda
Akiko
A
Longnecker
Richard
R
D000818:Animals; D000911:Antibodies, Monoclonal; D001665:Binding Sites; D004854:Herpesvirus 4, Human / Q000378:metabolism*; D051379:Mice; D009088:Mucoproteins; D010957:Plasmids; D051381:Rats; D014162:Transfection; D014407:Tumor Cells, Cultured; D025801:Ubiquitin / Q000378:metabolism*; D014763:Viral Matrix Proteins / Q000378:metabolism*
D000911:Antibodies, Monoclonal; C037662:EBV-associated membrane antigen, Epstein-Barr virus; D009088:Mucoproteins; D025801:Ubiquitin; D014763:Viral Matrix Proteins; C010393:lysin, gastropoda