Microtubule disruption stimulates P-body formation

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Updated: Jul 16, 2026

Self-Assembly of Microtubule Tactoids
08:49

Self-Assembly of Microtubule Tactoids

Published on: June 23, 2022

Thomas J Sweet1, Brooke Boyer, Wenqian Hu

  • 1Center for RNA Molecular Biology, Case Western Reserve University, Cleveland, OH 44106, USA.

RNA (New York, N.Y.)
|February 20, 2007
PubMed

Insights

Processing bodies (P-bodies) aggregate with microtubule disruption in yeast. This P-body formation is independent of global mRNA decay or translation changes, revealing a link to the microtubule network.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Yeast Genetics

Background:

  • Processing bodies (P-bodies) are conserved RNP granules involved in mRNA metabolism, but their formation mechanisms remain unclear.
  • P-bodies are dynamic structures whose formation correlates with mRNA metabolism changes.
  • The relationship between P-bodies and the cellular cytoskeleton is not well understood.

Purpose of the Study:

  • To investigate the relationship between P-bodies and microtubules in Saccharomyces cerevisiae.
  • To determine if microtubule disruption affects P-body formation and composition.
  • To explore the functional consequences of microtubule-induced P-body aggregation.

Main Methods:

  • Disruption of microtubules using the drug benomyl and a temperature-sensitive alpha-tubulin mutant (tub1-724).
  • Assessment of P-body component aggregation and colocalization with alpha-tubulin (Tub1).
  • Identification of P-body protein components using yeast genetics and analysis of YBR094W.
  • Measurement of global mRNA stability and translation levels following microtubule disruption.

Main Results:

  • Disruption of microtubules by benomyl or the tub1-724 mutation leads to P-body component aggregation and stimulates P-body formation.
  • The alpha-tubulin protein Tub1 colocalizes with P-bodies upon microtubule destabilization.
  • A putative tubulin tyrosine ligase (YBR094W) is identified as a P-body component.
  • Microtubule-induced P-body formation does not correlate with global changes in mRNA stability or translation.

Conclusions:

  • P-body aggregation is directly linked to the integrity of the intracellular microtubule network in yeast.
  • Microtubule destabilization induces P-body formation independently of broad changes in mRNA decay or translation.
  • These findings establish a physical connection between P-bodies and the microtubule cytoskeleton.

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