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Related Concept Videos

NF-κB-dependent Signaling Pathway02:26

NF-κB-dependent Signaling Pathway

The transcription factor NF-κB was discovered in 1986 in the lab of Nobel laureate Professor David Baltimore, for its interaction with the immunoglobulin light chain enhancer in B-cells. After more than three decades of study, it is now evident that NF-κB regulates the expression of over 100 genes. Most of these genes play an essential role in the innate and adaptive immune responses as well as the inflammatory responses of animals.
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The JAK-STAT Signaling Pathway

Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
Co-activators and Co-repressors02:04

Co-activators and Co-repressors

Gene transcription is regulated by the synergistic action of several proteins that form a complex at a gene regulatory site. This is observed in eukaryotes, where the regulation of gene expression is a complex process. Regulatory proteins in eukaryotes can broadly be classified into two types – regulators that bind directly to specific DNA sequences and co-regulators that associate with regulatory proteins but cannot directly bind to the DNA. These co-regulators are further divided into...
NF-kB-dependent Signaling Pathway02:26

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Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...

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NF-κB-dependent Luciferase Activation and Quantification of Gene Expression in Salmonella Infected Tissue Culture Cells
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NF-κB repression by PIAS3 mediated RelA SUMOylation.

Yuangang Liu1, Rebecca Bridges, Aaron Wortham

  • 1Department of Dermatology, Oregon Health and Science University, Portland, Oregon, United States of America. liuy@ohsu.edu

Plos One
|June 1, 2012
PubMed
Summary

Nuclear factor-kappa B (NF-κB) is negatively regulated by SUMOylation. PIAS3 ligase SUMOylates the RelA subunit of NF-κB, forming a negative feedback loop for homeostasis.

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • Nuclear factor-kappa B (NF-κB) is a crucial transcription factor for tissue homeostasis.
  • NF-κB activity is modulated by post-translational modifications like phosphorylation, acetylation, and ubiquitination.

Purpose of the Study:

  • To investigate the role of SUMOylation in regulating NF-κB activity.
  • To identify the specific proteins involved in NF-κB SUMOylation.

Main Methods:

  • Experimental evidence for NF-κB SUMOylation was provided.
  • The E3 SUMO ligase activity of PIAS3 in regulating NF-κB was examined.
  • Mutant analysis of RelA and PIAS3 was performed.

Main Results:

  • The RelA subunit of NF-κB was found to be SUMOylated by PIAS3.
  • PIAS3-mediated repression of NF-κB was dependent on SUMOylation.
  • NF-κB activation induced PIAS3-mediated SUMOylation of RelA, creating a negative feedback loop.
  • RelA DNA binding was identified as a signal for PIAS3-mediated SUMOylation.

Conclusions:

  • NF-κB is regulated by SUMOylation via the PIAS3 ligase.
  • PIAS3-mediated RelA SUMOylation represents a novel negative feedback mechanism for NF-κB regulation.