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Inhibition of Canonical NF-κB Signaling by a Small Molecule Targeting NEMO-Ubiquitin Interaction.

Abstract：

:The IκB kinase (IKK) complex acts as the gatekeeper of canonical NF-κB signaling, thereby regulating immunity, inflammation and cancer. It consists of the catalytic subunits IKKα and IKKβ and the regulatory subunit NEMO/IKKγ. Here, we show that the ubiquitin binding domain (UBAN) in NEMO is essential for IKK/NF-κB activation in response to TNFα, but not IL-1β stimulation. By screening a natural compound library we identified an anthraquinone derivative that acts as an inhibitor of NEMO-ubiquitin binding (iNUB). Using biochemical and NMR experiments we demonstrate that iNUB binds to NEMOUBAN and competes for interaction with methionine-1-linked linear ubiquitin chains. iNUB inhibited NF-κB activation upon UBAN-dependent TNFα and TCR/CD28, but not UBAN-independent IL-1β stimulation. Moreover, iNUB was selectively killing lymphoma cells that are addicted to chronic B-cell receptor triggered IKK/NF-κB activation. Thus, iNUB disrupts the NEMO-ubiquitin protein-protein interaction interface and thereby inhibits physiological and pathological NF-κB signaling.

journal_name

Sci Rep

journal_title

Scientific reports

authors

Vincendeau M,Hadian K,Messias AC,Brenke JK,Halander J,Griesbach R,Greczmiel U,Bertossi A,Stehle R,Nagel D,Demski K,Velvarska H,Niessing D,Geerlof A,Sattler M,Krappmann D

doi

10.1038/srep18934

subject

Has Abstract

pub_date

2016-01-07 00:00:00

pages

18934

issn

2045-2322

pii

srep18934

journal_volume

6

pub_type

杂志文章

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