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AKT1 — 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