Dynamics of Tpm1.8 domains on actin filaments with single-molecule resolution-Reference-Cited by-同舟云学术

Dynamics of Tpm1.8 domains on actin filaments with single-molecule resolution

Published:2020-10-15 Issue:22 Volume:31 Page:2452-2462
ISSN:1059-1524
Container-title:Molecular Biology of the Cell
language:en
Short-container-title:MBoC

Author:

Bareja Ilina¹,Wioland Hugo²,Janco Miro¹,Nicovich Philip R.¹,Jégou Antoine²,Romet-Lemonne Guillaume²,Walsh James¹,Böcking Till¹

Affiliation:

1. EMBL Australia Node in Single Molecule Science and ARC Centre of Excellence in Advanced Molecular Imaging, School of Medical Sciences, UNSW Sydney, Sydney, NSW 2052, Australia

2. Université de Paris, CNRS, Institut Jacques Monod, 75006 Paris, France

Abstract

Characterization of the kinetics of Tpm1.8 binding to actin filaments with single-molecule resolution. This work provides molecular insight into actin–tropomyosin filament formation and the role of tropomyosins in regulating actin filament dynamics.

Publisher

American Society for Cell Biology (ASCB)

Subject

Cell Biology,Molecular Biology

Reference48 articles.

1. Recruitment Kinetics of Tropomyosin Tpm3.1 to Actin Filament Bundles in the Cytoskeleton Is Independent of Actin Filament Kinetics

2. Tropomyosin Promotes Lamellipodial Persistence by Collaborating with Arp2/3 at the Leading Edge

3. Analysis of biophysical and functional consequences of tropomyosin-fluorescent protein fusions

4. Specification of Actin Filament Function and Molecular Composition by Tropomyosin Isoforms

5. Actin Filament Dynamics Using Microfluidics

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