Literature DB >> 17208983

Attachment conditions control actin filament buckling and the production of forces.

Julien Berro1, Alphée Michelot, Laurent Blanchoin, David R Kovar, Jean-Louis Martiel.   

Abstract

Actin polymerization is the driving force for a large number of cellular processes. Formation of lamellipodia and filopodia at the leading edge of motile cells requires actin polymerization induced mechanical deformation of the plasma membrane. To generate different types of membrane protrusions, the mechanical properties of actin filaments can be constrained by interacting proteins. A striking example of such constraint is the buckling of actin filaments generated in vitro by the cooperative effect of a processive actin nucleating factor (formin) and a molecular motor (myosin II). We developed a physical model based on equations for an elastic rod that accounts for actin filament buckling. Both ends of the rod were maintained in a fixed position in space and we considered three sets of boundary conditions. The model qualitatively and quantitatively reproduces the shape distribution of actin filaments. We found that actin polymerization counterpoises a force in the range 0.4-1.6 pN for moderate end-to-end distance (approximately 1 microm) and could be as large as 10 pN for shorter distances. If the actin rod attachment includes a spring, we discovered that the stiffness must be in the range 0.1-1.2 pN/nm to account for the observed buckling.

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Year:  2007        PMID: 17208983      PMCID: PMC1864840          DOI: 10.1529/biophysj.106.094672

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  34 in total

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Authors:  Thomas D Pollard; Gary G Borisy
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3.  Actin polymerization-driven molecular movement of mDia1 in living cells.

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Journal:  Cell       Date:  2004-10-29       Impact factor: 41.582

5.  Multiple- and single-molecule analysis of the actomyosin motor by nanometer-piconewton manipulation with a microneedle: unitary steps and forces.

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7.  The stiffness of rabbit skeletal actomyosin cross-bridges determined with an optical tweezers transducer.

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9.  Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments.

Authors:  T D Pollard
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  20 in total

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Journal:  Biophys J       Date:  2015-11-03       Impact factor: 4.033

2.  Actin Filament Strain Promotes Severing and Cofilin Dissociation.

Authors:  Anthony C Schramm; Glen M Hocky; Gregory A Voth; Laurent Blanchoin; Jean-Louis Martiel; Enrique M De La Cruz
Journal:  Biophys J       Date:  2017-06-20       Impact factor: 4.033

3.  Compressing a rigid filament: buckling and cyclization.

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Journal:  Eur Phys J E Soft Matter       Date:  2007-11-09       Impact factor: 1.890

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6.  Filamentous network mechanics and active contractility determine cell and tissue shape.

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7.  Mechanical heterogeneity favors fragmentation of strained actin filaments.

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Journal:  Biophys J       Date:  2015-05-05       Impact factor: 4.033

8.  Plastic Deformation and Fragmentation of Strained Actin Filaments.

Authors:  Anthony C Schramm; Glen M Hocky; Gregory A Voth; Jean-Louis Martiel; Enrique M De La Cruz
Journal:  Biophys J       Date:  2019-06-25       Impact factor: 4.033

9.  Cofilin-linked changes in actin filament flexibility promote severing.

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10.  A mechanochemical model of actin filaments.

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