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Anti-IKK alpha, phospho (Ser180) / IKK beta, phospho (Ser181) Antibody, Unconjugated

RRID:AB_331624

Antibody ID

AB_331624

Target Antigen

IKK alpha, phospho (Ser180) / IKK beta, phospho (Ser181) human, mouse, rat

Proper Citation

(Cell Signaling Technology Cat# 2681, RRID:AB_331624)

Clonality

unknown

Comments

manufacturer recommendations: Immunocytochemistry; Western Blot; Western Blotting

Vendor

Cell Signaling Technology

Cat Num

2681

Publications that use this research resource

A constitutively-active IKK-complex at the axon initial segment.

  • König HG
  • Brain Res.
  • 2018 Jan 1

Literature context: /β, 1:500, scbt, Cat# sc-23470, RRID:AB_331624), a goat polyclonal anti-Ser177


Abstract:

BACKGROUND: Previous studies provided evidence for an accumulation of IκB-kinase (IKK) α/β at the axon initial segment (AIS), a neuronal compartment defined by ankyrin-G expression. Here we explored whether the presence of the IKK-complex at the AIS was associated with the activation of IKK signaling at this site. METHODS AND RESULTS: Proximity-ligation assays (PLAs) using pan-IKKα/β, phospho-IKKα/β-specific as well as ankyrin-G specific antibodies validated their binding to proximal epitopes in the AIS, while antibodies to other phosphorylated signaling proteins showed no preference for the AIS. Small-hairpin mediated silencing of IKKβ significantly reduced anti-phospho-IKKα/β-immunoreactivities in the AIS. ank3 gene-deficient cerebellar Purkinje cells also exhibited no phosphorylated IKKα/β at the proximal region of their axons. Transient ankyrin-G overexpression in PC12 cells augmented NF-κB transactivation in an ankyrin-G death-domain dependent manner. Finally, small molecule inhibitors of IKK-activity, including Aspirin, inhibited the accumulation of activated IKK proteins in the AIS. CONCLUSION: Our data suggest the existence of a constitutively-active IKK signaling complex in the AIS.

YOD1/TRAF6 association balances p62-dependent IL-1 signaling to NF-κB.

  • Schimmack G
  • Elife
  • 2017 Feb 28

Literature context: (RRID:AB_331624), JNK1/2 (


Abstract:

The ubiquitin ligase TRAF6 is a key regulator of canonical IκB kinase (IKK)/NF-κB signaling in response to interleukin-1 (IL-1) stimulation. Here, we identified the deubiquitinating enzyme YOD1 (OTUD2) as a novel interactor of TRAF6 in human cells. YOD1 binds to the C-terminal TRAF homology domain of TRAF6 that also serves as the interaction surface for the adaptor p62/Sequestosome-1, which is required for IL-1 signaling to NF-κB. We show that YOD1 competes with p62 for TRAF6 association and abolishes the sequestration of TRAF6 to cytosolic p62 aggregates by a non-catalytic mechanism. YOD1 associates with TRAF6 in unstimulated cells but is released upon IL-1β stimulation, thereby facilitating TRAF6 auto-ubiquitination as well as NEMO/IKKγ substrate ubiquitination. Further, IL-1 triggered IKK/NF-κB signaling and induction of target genes is decreased by YOD1 overexpression and augmented after YOD1 depletion. Hence, our data define that YOD1 antagonizes TRAF6/p62-dependent IL-1 signaling to NF-κB.