Public Library of Science
Proteasomal inhibition triggers viral oncoprotein degradation via autophagy-lysosomal pathway
Schematic representation of proteasomal inhibition mediated EBNA3C’s degradation.
EBNA3C expressing B-cells are more sensitive to apoptotic cell death induced by proteasome inhibitors.
Proteasome inhibitors can be used as potential therapeutic strategy against EBV associated B-cell lymphomas.
EBNA3C N-terminal domain is degraded in both nuclear and cytoplsamic fractions upon proteasomal inhibition.
N-terminal domain of EBNA3C is important for autophagy mediated degradation in response to proteasomal inhibition.
EBNA3C is predominantly K63-linked polyubiquitinated when proteasome is inhibited.
EBNA3C participates within the p62-LC3B complex when proteasome is inhibited.
EBNA3C is degraded through autophagy-lysosomal pathway when proteasome is inhibited.
Proteasomal inhibition induces both viral and autophagy gene transcriptions.