IndraLab

Statements

USP11 binds eIF. 8 / 8
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"Moreover, phosphorylation of p70-RSK was noted to be reduced in ABC-, but not in GC-DLBCLs, upon either C75 treatment or FASN depletion, indicating that active p70-RSK may be driving the USP11-eIF4B interaction for sustained oncogene expression (Supplementary Figure  xref )."
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"The interaction of USP11 with eIF4B, a protein that interacts and promotes the activity of eIF4A, implicated its role in regulating de novo peptide synthesis."
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"One novel potential lymphoma-associated driver of eIF4B is fatty acid synthase (FASN) which stabilizes eIF4B and increase expression of oncoproteins such as MYC, BCL6 and MCL1 (a BCL2-related anti-apoptotic protein) via formation of a complex between eIF4B and the deubiquitinase USP11 in DLBCL cells [ xref ]."
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"We previously reported that USP11, a bona fide eIF4B deubiquitinase, is phospho-modified by p70-S6Kinase and this post-translational event enhances USP11-eIF4B interactions( xref )."
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"Finally, the interaction between eIF4B and USP11 is directly modulated by FASN-mediated S6Kinase activity (Fig.  xref )."
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"Our previous report( xref ) noted that FASN activated PI3K signaling tethered USP11-eIF4B interactions."
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"We showed before that fatty acid synthase is involved with DLBCL progression in part by inducing PI3K-Akt-S6Kinase signaling to enhance interactions a USP11-eIF4B complex xref ."
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"In light of this apparently conflicting observation based on in vitro and cell-based deubiquitination assays, we next examined whether the interaction between USP11 and eIF4B was S6Kinase-dependent."
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