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After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
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IKKγ/NEMO Localization into Multivesicular Bodies.

Lisa-Marie Wackernagel1, Mohsen Abdi Sarabi1, Sönke Weinert1

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International Journal of Molecular Sciences
|June 24, 2022
PubMed
Summary

Glycogen synthase kinase-3β (GSK-3β) regulates nuclear factor-kappa B (NF-κB) pathway activation by controlling NEMO localization to endosomes. Vps4A and V-ATPase are crucial for NEMO stability and NF-κB signaling.

Keywords:
NF-κB essential modifier (NEMO/IKKγ)NF-κB pathwayglycogen synthase kinase-3 (GSK-3)

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Nano-fEM: Protein Localization Using Photo-activated Localization Microscopy and Electron Microscopy
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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Immunology

Background:

  • The nuclear factor-kappa B (NF-κB) pathway is critical for inflammatory and immune responses.
  • IKKγ/NEMO is essential for NF-κB activation, and glycogen synthase kinase-3β (GSK-3β) regulates this process.
  • Previous work identified GSK-3β's role in NF-κB activation via IKKγ/NEMO regulation.

Purpose of the Study:

  • To elucidate the precise mechanism by which GSK-3β regulates NF-κB activation.
  • To investigate the role of endosomal trafficking and associated proteins in NF-κB signaling.
  • To identify novel regulators of NEMO stability and NF-κB pathway activation.

Main Methods:

  • Utilized siRNA to identify the AAA-ATPase Vps4A.
  • Employed co-immunoprecipitation to study NEMO and Vps4A interactions.
  • Observed endosomal localization using the endosome marker Rab5.
  • Investigated the effects of Vps4A mutants and bafilomycin A treatment on NEMO expression and NF-κB activation.

Main Results:

  • GSK-3β phosphorylation induces NEMO localization into multivesicular bodies (MVBs) and endosomes.
  • Vps4A is identified as essential for NEMO stability and NF-κB activation, interacting directly with phosphorylated NEMO.
  • Constitutively active Vps4A enhances NEMO expression and NF-κB activation.
  • Bafilomycin A treatment downregulates NEMO and inhibits NF-κB signaling, highlighting V-ATPase involvement.

Conclusions:

  • GSK-3β plays a key role in NF-κB activation through NEMO phosphorylation and subsequent endosomal trafficking.
  • Vps4A is a novel, essential component for NEMO stability and NF-κB pathway function.
  • V-ATPase activity is required for maintaining NEMO levels and sustaining NF-κB signal transduction.
  • These findings reveal an unexpected regulatory role for endosomal trafficking machinery in NF-κB signaling.