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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.
NF-κB-dependent Signaling Mechanism
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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...
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...
NF-kB-dependent Signaling Pathway02:26

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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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Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

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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Transducer Mechanism: Nuclear Receptors

Nuclear receptors, or NRs, are unique transcription factors that regulate gene transcription and affect the cellular pathways involved in reproduction, development, or metabolism. Their ability to be stimulated by small lipophilic ligands and control vital cellular processes makes them ideal drug targets. Nearly 10-15% of currently prescribed drugs target these receptors.
About 48 different soluble family members of nuclear receptors are identified that can be divided into two main classes:

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NF-κB-dependent Luciferase Activation and Quantification of Gene Expression in Salmonella Infected Tissue Culture Cells
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A structural basis for selective dimerization by NF-κB RelB.

Don Vu1, De-Bin Huang1, Annapurna Vemu1

  • 1Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0375, USA.

Journal of Molecular Biology
|March 15, 2013
PubMed
Summary

RelB, a nuclear factor kappaB (NF-κB) subunit, selectively forms heterodimers. Specific mutations reveal how RelB

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Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Nuclear factor kappaB (NF-κB) transcription factors regulate immune responses and development.
  • NF-κB proteins form functional dimers from five distinct Rel subunits.
  • The RelB subunit typically forms heterodimers, not homodimers, with p50 or p52.

Purpose of the Study:

  • To elucidate the structural mechanisms underlying selective dimerization of NF-κB Rel subunits.
  • To understand why RelB does not naturally form homodimers.
  • To investigate the role of specific amino acid residues in RelB dimerization.

Main Methods:

  • X-ray crystallography was used to determine the structures of five RelB dimers.
  • Site-directed mutagenesis was employed to alter specific residues in the RelB dimerization domain.
  • Analysis of canonical and non-canonical dimer interfaces.

Main Results:

  • RelB forms canonical side-by-side heterodimers with p50 and p52.
  • Mutating four surface hydrophobic residues did not induce RelB homodimerization.
  • Altering two interfacial residues forced RelB into a distinct side-by-side homodimer conformation.
  • Mutant RelB homodimers exhibited altered monomer spacing to avoid unfavorable interactions.

Conclusions:

  • Specific amino acid residues within the RelB dimerization domain dictate its heterodimer preference.
  • The hydrophobic core of the RelB domain influences surface residue conformations and dimerization.
  • RelB has evolved unique residues for selective heterodimerization with p50 and p52, contributing to NF-κB pathway specificity.