Rotational movement of the formin mDia1 along the double helical strand of an actin filament

Hiroaki Mizuno, Chiharu Higashida, Yunfeng Yuan, Toshimasa Ishizaki, Shuh Narumiya, Naoki Watanabe

Research output: Contribution to journalArticle

76 Citations (Scopus)

Abstract

Formin homology proteins (formins) elongate actin filaments (F-actin) by continuously associating with filament tips, potentially harnessing actin-generated pushing forces. During this processive elongation, formins are predicted to rotate along the axis of the double helical F-actin structure (referred to here as helical rotation), although this has not yet been definitively shown. We demonstrated helical rotation of the formin mDia1 by single-molecule fluorescence polarization (FLP). FLP of labeled F-actin, both elongating and depolymerizing from immobilized mDia1, oscillated with a periodicity corresponding to that of the F-actin long-pitch helix, and this was not altered by actin-bound nucleotides or the actin-binding protein profilin. Thus, helical rotation is an intrinsic property of formins. To harness pushing forces from growing F-actin, formins must be anchored flexibly to cell structures.

Original languageEnglish
Pages (from-to)80-83
Number of pages4
JournalScience
Volume331
Issue number6013
DOIs
Publication statusPublished - 2011 Jan 7
Externally publishedYes

ASJC Scopus subject areas

  • General

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    Mizuno, H., Higashida, C., Yuan, Y., Ishizaki, T., Narumiya, S., & Watanabe, N. (2011). Rotational movement of the formin mDia1 along the double helical strand of an actin filament. Science, 331(6013), 80-83. https://doi.org/10.1126/science.1197692