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Actin-capping protein promotes microtubule stability by antagonizing the actin activity of mDia1

Francesca Bartolini1, Nagendran Ramalingam, Gregg G Gundersen

  • 1Department of Pathology and Cell Biology, Columbia University, New York, NY 10032, USA.

Molecular Biology of the Cell
|August 25, 2012
PubMed

Insights

Actin-capping protein regulates microtubule (MT) stability by modulating mDia1 activity. This study reveals a novel cross-talk mechanism between actin and MTs.

Area of Science:

  • Cell Biology
  • Cytoskeleton Dynamics
  • Molecular Cell Biology

Background:

  • RhoA and its effector mDia1 are crucial for stabilizing microtubules (MTs) during fibroblast migration.
  • The dual role of mDia1 in actin polymerization and MT stabilization, and their interplay, remains unclear.

Purpose of the Study:

  • To investigate the relationship between mDia1's actin-binding and MT-stabilizing activities.
  • To identify physiological regulators of mDia1's function in MT stabilization.
  • To elucidate the mechanism of actin-microtubule cross-talk.

Main Methods:

  • Utilized actin drugs (latrunculin A, jasplakinolide) to modulate mDia1 localization.
  • Employed small interfering RNA (siRNA) for knockdown of mDia1 and actin-capping protein.
  • Investigated effects of Rho and integrin signaling inhibition.
  • Assessed stable MT formation and mDia1 redistribution.

Main Results:

  • Actin drugs releasing mDia1 from actin filaments promoted stable MT formation and mDia1 redistribution onto MTs.
  • mDia1 knockdown abrogated LatA-induced stable MT formation.
  • Actin-capping protein induced stable MTs via mDia1 and inhibited mDia1 translocation on actin filaments.
  • Capping protein knockdown reduced stable MT levels in proliferating and starved cells.

Conclusions:

  • Actin-capping protein is a novel regulator of MT stability.
  • It functions by antagonizing mDia1's actin-binding activity, indirectly promoting MT stabilization.
  • This study reveals a new mechanism of actin-MT cross-talk involving sequential regulation of actin and MTs by a single factor.

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