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Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO
Published on: December 28, 2019
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Structurally plastic NEMO and oligomerization prone IKK2 subunits define the behavior of human IKK2:NEMO complexes in
Myung Soo Ko1, Tapan Biswas2, Maria Carmen Mulero3
1Structural Biochemistry Laboratory, Department of Chemistry & Biochemistry, San Diego State University, 5500 Campanile Drive, San Diego, CA 92182-1030, United States; Department of Chemistry & Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0357, United States.
Biochimica Et Biophysica Acta. Proteins and Proteomics
|August 28, 2020
Summary
The NEMO/IKKγ subunit
Area of Science:
- Molecular Biology
- Structural Biology
- Biochemistry
Background:
- The IκB Kinase (IKK) complex regulates transcription factor NF-κB activity.
- IKK complex subunits include catalytic kinases (IKK1/IKKα, IKK2/IKKβ) and scaffolding NEMO/IKKγ.
- IKK subunits homo-oligomerize, influencing catalytic activity and NF-κB pathway activation.
Purpose of the Study:
- To investigate the solution behavior and structural dynamics of the NEMO/IKKγ subunit.
- To understand how NEMO influences the structural properties and oligomerization of the IKK complex.
Main Methods:
- Size-exclusion chromatography
- Multi-angle light scattering
- Analytical centrifugation
- Thermal denaturation analyses
Main Results:
- NEMO predominantly exists as a dimer in solution but exhibits complex dynamics due to its coiled-coil regions.
- These dynamics cause NEMO to appear as a larger particle in solution.
- Within the IKK2 complex, NEMO maintains its dynamic character and promotes IKK2 homo-oligomerization.
Conclusions:
- NEMO's structural plasticity is crucial for IKK complex regulation and NF-κB signaling.
- Understanding NEMO's dynamics clarifies its role in disease pathogenesis.
- Oligomerization-dependent phosphorylation of IKK2 is modulated by NEMO's structural properties.
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