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Visualizing dynamic actin cross‐linking processes driven by the actin‐binding protein anillin
Author(s) -
Matsuda Kyohei,
Sugawa Mitsuhiro,
Yamagishi Masahiko,
Kodera Noriyuki,
Yajima Junichiro
Publication year - 2020
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13720
Subject(s) - protein filament , actin , cytokinesis , formins , actin binding protein , total internal reflection fluorescence microscope , actin remodeling , biophysics , chemistry , fluorescence microscope , filamin , actin cytoskeleton , cytoskeleton , microscopy , fluorescence , biology , physics , cell division , optics , biochemistry , cell
Anillin is a type of actin filament cross‐linking protein that stabilizes the actin‐based contractile ring during cytokinesis. To elucidate the underlying intermolecular interactions between actin filaments and anillin, we utilized total internal reflection fluorescence microscopy (TIRFM) and high‐speed atomic force microscopy (Hs‐AFM). Single‐molecule imaging of anillin using TIRFM showed that anillin exists as monomers with relatively low binding affinity for actin filaments. Real‐time imaging of actin filament cross‐linking dynamics induced by anillin using Hs‐AFM revealed that anillin monomers cross‐link with actin filaments at a distance of 8 nm and that the polarity of those filaments is both parallel and antiparallel. These results are consistent with anillin playing a role in actin ring transition in vivo , where it might be responsible for thinning the ring‐shaped apolar actin bundles.