Two opposite effects of cofilin on the thermal unfolding of F-actin: a differential scanning calorimetric study

Irina V. Dedova, Olga P. Nikolaeva, Valeria V. Mikhailova, Cris G. dos Remedios, Dmitrii I. Levitsky*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

40 Citations (Scopus)

Abstract

Differential scanning calorimetry was used to examine the effects of cofilin on the thermal unfolding of actin. Stoichiometric binding increases the thermal stability of both G- and F-actin but at sub-saturating concentrations cofilin destabilizes F-actin. At actin:cofilin molar ratios of 1.5-6 the peaks corresponding to stabilized (66-67°C) and destabilized (56-57°C) F-actin are observed simultaneously in the same thermogram. Destabilizing effects of sub-saturating cofilin are highly cooperative and are observed at actin:cofilin molar ratios as low as 100:1. These effects are abolished by the addition of phalloidin or aluminum fluoride. Conversely, at saturating concentrations, cofilin prevents the stabilizing effects of phalloidin and aluminum fluoride on the F-actin thermal unfolding. These results suggest that cofilin stabilizes those actin subunits to which it directly binds, but destabilizes F-actin with a high cooperativity in neighboring cofilin-free regions.

Original languageEnglish
Pages (from-to)119-128
Number of pages10
JournalBiophysical Chemistry
Volume110
Issue number1-2
DOIs
Publication statusPublished - 1 Jul 2004
Externally publishedYes

Keywords

  • Actin
  • ADF, actin depolymerizing factor
  • Cofilin
  • Differential scanning calorimetry
  • DSC, differential scanning calorimetry.
  • Thermal unfolding

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