Literature DB >> 35773996

How torque on formins is relaxed strongly affects cellular swirling.

Xi Li1, Bin Chen2.   

Abstract

Chirality is a common and essential characteristic at varied scales of living organisms. By adapting the rotational clutch-filament model we previously developed, we investigate the effect of torque relaxation of a formin on cellular chiral swirling. Since it is still unclear how the torque on a formin is exactly relaxed, we probe three types of torque relaxation, as suggested in the literature. Our analysis indicates that, when a formin periodically undergoes positive and negative rotation during processive capping to relax the torque, cells hardly rotate. When the switch between the positive and the negative rotation during the processive capping is randomly regulated by the torque, our analysis indicates that cells can only slightly rotate either counterclockwise or clockwise. When a formin relaxes the torque by transiently loosening its contact either with the membrane at its anchored site or with the actin filament, we find that cells can prominently rotate either counterclockwise or clockwise, in good consistency with the experiment. Thus, our studies indicate that how the torque on a formin is relaxed strongly affects cellular swirling and suggest an efficient type of torque relaxation in switching cellular swirling.
Copyright © 2022 Biophysical Society. Published by Elsevier Inc. All rights reserved.

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Year:  2022        PMID: 35773996      PMCID: PMC9388394          DOI: 10.1016/j.bpj.2022.06.027

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   3.699


  39 in total

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

Authors:  Hiroaki Mizuno; Chiharu Higashida; Yunfeng Yuan; Toshimasa Ishizaki; Shuh Narumiya; Naoki Watanabe
Journal:  Science       Date:  2010-12-09       Impact factor: 47.728

2.  A novel mechanism of actin filament processive capping by formin: solution of the rotation paradox.

Authors:  Tom Shemesh; Takanori Otomo; Michael K Rosen; Alexander D Bershadsky; Michael M Kozlov
Journal:  J Cell Biol       Date:  2005-09-12       Impact factor: 10.539

Review 3.  Left-right asymmetry in embryonic development: a comprehensive review.

Authors:  Michael Levin
Journal:  Mech Dev       Date:  2005-01       Impact factor: 1.882

4.  Crystal structure of the alpha-actinin rod reveals an extensive torsional twist.

Authors:  J Ylänne; K Scheffzek; P Young; M Saraste
Journal:  Structure       Date:  2001-07-03       Impact factor: 5.006

5.  Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm.

Authors:  M Lorenz; D Popp; K C Holmes
Journal:  J Mol Biol       Date:  1993-12-05       Impact factor: 5.469

6.  A conserved mechanism for Bni1- and mDia1-induced actin assembly and dual regulation of Bni1 by Bud6 and profilin.

Authors:  James B Moseley; Isabelle Sagot; Amity L Manning; Yingwu Xu; Michael J Eck; David Pellman; Bruce L Goode
Journal:  Mol Biol Cell       Date:  2003-12-02       Impact factor: 4.138

Review 7.  Review of the mechanism of processive actin filament elongation by formins.

Authors:  Aditya S Paul; Thomas D Pollard
Journal:  Cell Motil Cytoskeleton       Date:  2009-08

8.  Formin Is Associated with Left-Right Asymmetry in the Pond Snail and the Frog.

Authors:  Angus Davison; Gary S McDowell; Jennifer M Holden; Harriet F Johnson; Georgios D Koutsovoulos; M Maureen Liu; Paco Hulpiau; Frans Van Roy; Christopher M Wade; Ruby Banerjee; Fengtang Yang; Satoshi Chiba; John W Davey; Daniel J Jackson; Michael Levin; Mark L Blaxter
Journal:  Curr Biol       Date:  2016-02-25       Impact factor: 10.834

9.  mDia1 senses both force and torque during F-actin filament polymerization.

Authors:  Miao Yu; Xin Yuan; Chen Lu; Shimin Le; Ryo Kawamura; Artem K Efremov; Zhihai Zhao; Michael M Kozlov; Michael Sheetz; Alexander Bershadsky; Jie Yan
Journal:  Nat Commun       Date:  2017-11-21       Impact factor: 14.919

10.  Helical rotation of the diaphanous-related formin mDia1 generates actin filaments resistant to cofilin.

Authors:  Hiroaki Mizuno; Kotaro Tanaka; Sawako Yamashiro; Akihiro Narita; Naoki Watanabe
Journal:  Proc Natl Acad Sci U S A       Date:  2018-05-14       Impact factor: 11.205

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