Document Detail


Stochastic severing of actin filaments by actin depolymerizing factor/cofilin controls the emergence of a steady dynamical regime.
MedLine Citation:
PMID:  18065447     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Actin dynamics (i.e., polymerization/depolymerization) powers a large number of cellular processes. However, a great deal remains to be learned to explain the rapid actin filament turnover observed in vivo. Here, we developed a minimal kinetic model that describes key details of actin filament dynamics in the presence of actin depolymerizing factor (ADF)/cofilin. We limited the molecular mechanism to 1), the spontaneous growth of filaments by polymerization of actin monomers, 2), the ageing of actin subunits in filaments, 3), the cooperative binding of ADF/cofilin to actin filament subunits, and 4), filament severing by ADF/cofilin. First, from numerical simulations and mathematical analysis, we found that the average filament length, L, is controlled by the concentration of actin monomers (power law: 5/6) and ADF/cofilin (power law: -2/3). We also showed that the average subunit residence time inside the filament, T, depends on the actin monomer (power law: -1/6) and ADF/cofilin (power law: -2/3) concentrations. In addition, filament length fluctuations are approximately 20% of the average filament length. Moreover, ADF/cofilin fragmentation while modulating filament length keeps filaments in a high molar ratio of ATP- or ADP-P(i) versus ADP-bound subunits. This latter property has a protective effect against a too high severing activity of ADF/cofilin. We propose that the activity of ADF/cofilin in vivo is under the control of an affinity gradient that builds up dynamically along growing actin filaments. Our analysis shows that ADF/cofilin regulation maintains actin filaments in a highly dynamical state compatible with the cytoskeleton dynamics observed in vivo.
Authors:
Jeremy Roland; Julien Berro; Alphée Michelot; Laurent Blanchoin; Jean-Louis Martiel
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2007-12-07
Journal Detail:
Title:  Biophysical journal     Volume:  94     ISSN:  1542-0086     ISO Abbreviation:  Biophys. J.     Publication Date:  2008 Mar 
Date Detail:
Created Date:  2008-02-28     Completed Date:  2008-05-22     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  0370626     Medline TA:  Biophys J     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2082-94     Citation Subset:  IM    
Affiliation:
Université Joseph Fourier, TIMC-IMAG Laboratory, Grenoble, France.
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MeSH Terms
Descriptor/Qualifier:
Actins / chemistry,  physiology*
Adenosine Diphosphate / chemistry
Adenosine Triphosphate / chemistry
Cofilin 1 / chemistry*
Computer Simulation
Cytoskeleton / metabolism
Destrin / chemistry*
Kinetics
Microfilaments / chemistry,  metabolism*
Models, Biological
Models, Theoretical
Stochastic Processes
Chemical
Reg. No./Substance:
0/Actins; 0/Cofilin 1; 0/Destrin; 56-65-5/Adenosine Triphosphate; 58-64-0/Adenosine Diphosphate
Comments/Corrections

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