LMP2
Function
Isoform LMP2A
Maintains EBV latent infection of B-lymphocyte, by preventing lytic reactivation of the virus in response to surface immunoglobulin (sIg) cross-linking. Acts like a dominant negative inhibitor of the sIg-associated protein tyrosine kinases, LYN and SYK. Also blocks translocation of the B-cell antigen receptor (BCR) into lipid rafts, preventing the subsequent signaling and accelerated internalization of the BCR upon BCR cross-linking. Serves as a molecular scaffold to recruit SYK, LYN and E3 protein-ubiquitin ligases, such as ITCH and NEDD4L, leading to ubiquitination and potential degradation of both tyrosines kinases. Possesses a constitutive signaling activity in non-transformed cells, inducing bypass of normal B lymphocyte developmental checkpoints allowing immunoglobulin-negative cells to colonize peripheral lymphoid organs (By similarity).
Isoform LMP2B
May be a negative regulator of isoform LMP2A.
Post-translational modifications
Isoform LMP2A
Phosphorylated on cytoplasmic N-terminal tyrosine residues, possibly by human LYN.
Can be ubiquitinated by human ITCH and WWP2 on the N-terminus in a lysine-independent manner.
Sequence Similarities
Belongs to the herpesviridae LMP-2 family.
Cellular localization
- Isoform LMP2A
- Host cell membrane
- Multi-pass membrane protein
- Isoform LMP2A is localized in plasma membrane lipid rafts.
- Isoform LMP2B
- Host endomembrane system
- Multi-pass membrane protein
- Host cytoplasm
- Host perinuclear region
- Isoform LMP2B localizes to perinuclear regions.
Alternative names
Latent membrane protein 2, Terminal protein, LMP2