|Study||Cell lines||Patient Samples / animal studies||Treatment||Endpoints or objectives||Outcomes/Results|
|Li et al. ||CNE1, CNE-LMP1+||–||MG-132||Study of LMP1 regulating the expression of MDM2||MDM2 expression is upregulated by LMP1 through a post-ubiquitination mechanism.|
|Hau et al. ||HONE1, HONE1-EBV, CNE2-EBV C666–1, NP460-hTERT||–||MG-132||Examination of LMP1 protein levels in different EBV-infected cell lines||
- LMP1 protein is rapidly degraded via proteasome-mediated proteolysis.|
- Binding of Id1 to LMP1 suppressed polyubiquitination of LMP1 and may be involved in stabilization of LMP1 in EBV-infected nasopharyngeal epithelial cells.
-Proteasome inhibitor could effectively stabilize LMP1 protein in EBV-infected cells
- Id1 could interact and stabilize LMP1 by suppressing LMP1 polyubiquitination.
|Gainullin et al. ||CNE1, CNE2, TWO3, HONE1||
9 NPC tissues|
10 normal epithelial tissues from chronic nasopharyngitis patients
|MG-132||Role of LMP2A in the accumulation of cofilin in NPC.||
- LMP2A was found to interfere with cofilin degradation in NPC cells by accelerating the proteasomal degradation of Cbl and Syk.|
- Interference with cofilin degradation may enhance the metastatic potential of NPC cells
|Zhou et al. ||HONE1/Akata, HK1/Akata, C666–1, CNE1/Akata, CNE1 (EBV-)||
43 NPC tissues|
BALB/c nude mice
|Anti-cancer effect of triptolide and mechanism of EBNA1 in NPC cells||Low dose of triptolide reduce the half-life of EBNA1 and significantly decreased EBNA1 expression by promoting the process of proteasome ubiquitin pathway.|
|Zhang et al. ||
CNE1, CNE2, HNE1, HONE1, HK1, SUNE1, C666–1,|
Primary NPC cell lines
|–||–||Interplay between EBV gB and host proteins||
- FBXO2 ubiquitinates and degrades glycosylated gB.|
- Identification of SCFFBXO2 as an E3 ubiquitin ligase targeting EBV envelope protein gB.
|Meng et al. ||CNE1, CNE2 (S18, S26), SUNE-1 (5–8)||50 NPC tissues||MG132||Molecular mechanisms of NPC metastasis||
- S100A14 promoted the ubiquitin-proteasome-mediated degradation ofIRAK1 to suppress NPC cellular migration.|
- Lower S100A14 expression was significantly correlated with shorter patient OS and DMFS.
|Pan et al. ||CNE1, CNE2, HONE1, C666.1||
45 NPC tissues|
|Functional relationship between Jab1 and p27 protein expression||
- Jab1-mediated p27 degradation in a proteasome-dependent manner.|
- Overexpression of Jab1 correlated with poor survival in NPC patients.
|Liu et al. ||
|Effect of curcumin on the proliferation, cycle arrest, and apoptosis of EBV+ NPC cells||Curcumin induced EBNA1 degradation via the proteasome-ubiquitin pathway|
|Friboulet et al. ||
13 NPC biopsies|
C15 and C17 (EBV+ in nude mice) NPC xenografts
|Functions of c-IAP2 in NPC cells||- RMT 5265 induces the proteasome-mediated degradation of c-IAP2, resulting from the enhanced polyubiquitination of c-IAP2|
|Hui et al. ||HONE1, HK1-EBV, HONE1-EBV, HA, C666–1||Female BALB/c nude (nu/nu) mice||Bortezomib, SAHA (Vorinostat)||Mechanisms of apoptosis and effects on lytic cycle activation of EBV||
- Combination of bortezomib and SAHA synergistically induce killing of a panel of NPC cell lines and suppresses the growth of NPC xenografts in nude mice.|
- Bortezomib inhibits SAHA’s induction of EBV replication and abrogates production of infectious viral particles in NPC cells.
|Xu C. et al. ||NP69, CNE2, Hone1, C666–1||MG132||Mechanisms by which EBV elude immune responses||
- LMP1 inhibits Sendai virus mediated type I interferon production and downregulates RIG-I signaling pathway by promotion RIG-I degradation dependent on proteasome.|
- EBV employs a unique strategy to evade RIG-I mediated immune responses.
|Jiang et al. ||CNE2, CNE1||Bortezomib (PS-341)||Mechanism by which immune evasion affects the response to treatment of NPC.||
- Bortezomib downregulates IFNγ-induced IDO expression via inhibition of JAK/STAT1 signaling pathway.|
- Bortezomib can promote IkB-α phosphorylation-ubiquitination to release NF-kB from IkB-α.