Visualizing dynamic actin cross-linking processes driven by the actin-binding protein anillin.

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Matsuda K,Sugawa M,Yamagishi M,Kodera N,Yajima J

doi

10.1002/1873-3468.13720

subject

Has Abstract

pub_date

2020-04-01 00:00:00

pages

1237-1247

issue

8

eissn

0014-5793

issn

1873-3468

journal_volume

594

pub_type

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