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Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells
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Organelle Separation and Cell Signaling.

Leandro Silva Da Costa1,2, Damien Arnoult3,4

  • 1INSERM, UMR_S 1197, Hôpital Paul Brousse, 14 Avenue Paul Vaillant Couturier, 94807, Villejuif Cedex, France.

Methods in Molecular Biology (Clifton, N.J.)
|January 13, 2017
PubMed
Summary

This study reveals how ubiquitylated signaling molecules gather on organelles to control signal transduction. Simple immunoblotting methods are presented to observe these crucial ubiquitylated components in pathways like NF-κB and IRF3.

Keywords:
Cell fractionationDifferential centrifugationImmunoblottingSignalingUbiquitination

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Area of Science:

  • Cellular biology
  • Molecular signaling
  • Biochemistry

Background:

  • Signaling hubs are critical for cellular communication.
  • Ubiquitylated proteins play key roles in signal transduction.
  • Organelle-associated signaling is an emerging area of research.

Purpose of the Study:

  • To describe methods for observing ubiquitylated signaling components at organelle surfaces.
  • To assess the accumulation of ubiquitylated proteins in specific signaling pathways.

Main Methods:

  • Differential centrifugation to isolate organelles.
  • Immunoblotting to detect ubiquitylated proteins.
  • In vitro assays to analyze signaling components.

Main Results:

  • Ubiquitylated components of the NF-κB pathway were found to accumulate at the endoplasmic reticulum.
  • Ubiquitylated components of the IRF3 pathway were observed at the Golgi apparatus.
  • Established simple and effective methods for their detection.

Conclusions:

  • Organelle surfaces serve as platforms for signal transduction hubs.
  • Ubiquitylation is a key mechanism for organizing signaling complexes on organelles.
  • The described methods facilitate the study of organelle-associated signaling pathways.