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Related Experiment Videos

Quantitative Variations with pH of Actin Depolymerizing Factor/Cofilin's Multiple Actions on Actin Filaments.

Hugo Wioland1, Antoine Jegou1, Guillaume Romet-Lemonne1

  • 1Institut Jacques Monod, CNRS, Université Paris-Diderot , 75013 Paris , France.

Biochemistry
|December 1, 2018
PubMed
Summary

Actin depolymerizing factor (ADF)/cofilin

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Area of Science:

  • Cellular Biology
  • Biochemistry
  • Cytoskeleton Dynamics

Background:

  • Actin depolymerizing factor (ADF)/cofilin proteins regulate actin filament dynamics.
  • ADF/cofilin's efficiency is sensitive to pH, posing challenges in understanding its functions.
  • Cellular processes rely on precise control of actin filament assembly and disassembly.

Purpose of the Study:

  • Investigate ADF/cofilin's distinct reactions on actin filaments across a pH range.
  • Characterize ADF/cofilin's regulatory actions under specific biochemical conditions.
  • Elucidate the pH-dependent mechanisms of actin filament disassembly by ADF/cofilin.

Main Methods:

  • Employed single-filament microfluidics techniques.
  • Analyzed ADF/cofilin's interactions with actin filaments at four distinct pH values (6.6–7.8).

Related Experiment Videos

  • Quantified filament severing rates and depolymerization kinetics.

    • Main Results:

    • Decreasing pH reduces ADF/cofilin's filament severing rate by increasing filament saturation.
    • Severing rate per domain boundary remains constant across pH.
    • At physiological pH, ADF/cofilin drives rapid barbed-end depolymerization, while pointed-end depolymerization is minimally enhanced.

    Conclusions:

    • ADF/cofilin's severing activity is pH-dependent, primarily due to altered filament saturation.
    • Barbed-end depolymerization is the dominant contribution of ADF/cofilin at physiological pH.
    • Understanding ADF/cofilin's pH sensitivity is crucial for elucidating its role in cellular functions.