In-Cell Chemical Crosslinking Identifies Hotspots for SQSTM-1/p62-IκBα Interaction That Underscore a Critical Role of p62 in Limiting NF-κB Activation Through IκBα Stabilization

Liu, Yi; Trnka, Michael J.; Liang, He; Burlingame, Alma L.; Correia, Maria Almira

doi:10.1016/j.mcpro.2023.100495

Cited by 5 publications

(1 citation statement)

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“…A fascinating part of the story is the mechanism by which IκBα enters the nucleus, binds the NF-κB and returns it to the cytoplasm as the inactive NF-κB:IκBα complex. It had been thought that IκBα enters the nucleus by passive diffusion, but very recently in-cell cross-linking led to the discovery that SQSTM-1/p62 is a chaperone that ensures rapid translocation of newly synthesized IκBα into the nucleus [ 19 ].…”

Section: How Is Nf-κb Signaling Turned-off?mentioning

confidence: 99%

The multifunctional role of intrinsic disorder in NF-κB signaling

Komives

2023

Biochemical Society Transactions

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The nuclear factor-κB (NF-κB) transcription activation system involves disordered regions of both the NF-κB dimers and their inhibitors, the IκBs. The system is well-studied both at the cellular and biophysical levels affording a unique opportunity to compare and contrast the conclusions from both types of experiments. Through a combination of both experiments and theory, we have discovered that the RelA/p50 heterodimer and its inhibitor IκBα operate under kinetic control. Intrinsically disordered parts of both proteins are directly involved in temporal control and their folding and unfolding determines the rates of various processes. In this review, we show how the dynamic state of the intrinsically disordered sequences define the rates of intracellular processes.

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Section: How Is Nf-κb Signaling Turned-off?mentioning

confidence: 99%