TY - JOUR
T1 - Rotational movement of the formin mDia1 along the double helical strand of an actin filament
AU - Mizuno, Hiroaki
AU - Higashida, Chiharu
AU - Yuan, Yunfeng
AU - Ishizaki, Toshimasa
AU - Narumiya, Shuh
AU - Watanabe, Naoki
N1 - Copyright:
Copyright 2011 Elsevier B.V., All rights reserved.
PY - 2011/1/7
Y1 - 2011/1/7
N2 - 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.
AB - 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.
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U2 - 10.1126/science.1197692
DO - 10.1126/science.1197692
M3 - Article
C2 - 21148346
AN - SCOPUS:78650988290
VL - 331
SP - 80
EP - 83
JO - Science
JF - Science
SN - 0036-8075
IS - 6013
ER -