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AKT3 — PSMB9
Text-mined interactions from Literome
Scholle et al., J Virol 2000
(Cell Transformation, Neoplastic...) :
Epstein-Barr virus
LMP2A transforms epithelial cells, inhibits cell differentiation, and
activates Akt
Swart et al., J Virol 2000
(Burkitt Lymphoma) :
LMP2A expression
resulted in the constitutive phosphorylation of
Akt , and this LMP2A effect is dependent on phosphatidylinositol 3-kinase activity ... In addition, recruitment of Syk and Lyn protein tyrosine kinases ( PTKs ) to tyrosines 74 or 85 and 112, respectively, are critical for
LMP2A mediated
Akt phosphorylation
Morrison et al., J Virol 2003
:
LMP2A activates phosphatidylinositol 3-kinase (PI3K) and the serine/threonine kinase
Akt in lymphocytes and epithelial cells ...
LMP2A activated
Akt in a PI3K dependent manner, and the downstream Akt targets glycogen synthase kinase 3beta ( GSK3beta ) and the Forkhead transcription factor FKHR were phosphorylated and inactivated in LMP2A expressing HFK cells
Fukuda et al., J Virol 2004
(Burkitt Lymphoma) :
In this study, we found that
LMP2A induced the phosphorylation of
Akt ( serine 473 ) in Burkitt 's lymphoma cell line Ramos and in gastric carcinoma cell line HSC-39 and partially enhanced cell viability following TGF-beta 1 treatment
Moody et al., J Virol 2005
:
Expression of latency protein
LMP2A by the human tumor virus Epstein-Barr virus ( EBV )
activates phosphatidylinositol
3-kinase/Akt located upstream of an essential mediator of growth signals, mTOR ( mammalian target of rapamycin )
Matskova et al., Oncogene 2007
:
The Epstein-Barr virus latency associated membrane protein
LMP2A has been shown to
activate the survival kinase
Akt in epithelial and B cells in a phosphoinositide 3-kinase dependent fashion ... Our data set the precedent for viral utilization of the Shb signalling scaffold and implicate Shb as a regulator of
LMP2A dependent
Akt activation
Fukuda et al., J Virol 2007
(Cell Transformation, Viral) :
Furthermore, the Ras inhibitors manumycin A and a dominant negative form of Ras ( RasN17 ) and the PI3-K inhibitor LY294002 blocked
LMP2A mediated
Akt phosphorylation and anchorage independent cell growth in HSC-39 cells
Smith et al., Am J Physiol Endocrinol Metab 2008
(Sepsis...) :
Other important consequences of calpain activation that may contribute to muscle wasting during sepsis include degradation of certain transcription factors and nuclear cofactors,
activation of the
26S proteasome , and inhibition of
Akt activity, allowing for downstream activation of Foxo transcription factors and GSK-3beta
Siler et al., Virology 2008
:
The expression of rhesus
LMP2A in epithelial cells
induced Akt activation, GSK3beta inactivation and accumulation of beta-catenin in the cytoplasm and nucleus
Fotheringham et al., J Virol 2012
:
LMP2A induced Transwell migration required the Akt signaling pathway, and
activation of
Akt by
LMP2A required the ITAM signaling domain of LMP2A