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Crevenna, A.H.* ; Arciniega, M.* ; Dupont, A.* ; Mizuno, N.* ; Kowalska, K.* ; Lange, O.F. ; Wedlich-Soeldner, R.* ; Lamb, D.C.*

Side-binding proteins modulate actin filament dynamics.

eLife 4, DOI: 10.1101/008128 (2015)
Publ. Version/Full Text DOI PMC
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Actin filament dynamics govern many key physiological processes from cell motility to tissue morphogenesis. A central feature of actin dynamics is the capacity of the filament to polymerize and depolymerize at its ends in response to cellular conditions. It is currently thought that filament kinetics can be described by a single rate constant for each end. Here, using direct visualization of single actin filament elongation, we show that actin polymerization kinetics at both filament ends are strongly influenced by proteins that bind to the lateral filament surface. We also show that the less dynamic end, called the pointed-end, has a non-elongating state that dominates the observed filament kinetic asymmetry. Estimates of filament flexibility and Brownian dynamics simulations suggest that the observed kinetic diversity arises from structural alteration. Tuning filament kinetics by exploiting the natural malleability of the actin filament structure may be a ubiquitous mechanism to generate the rich variety of observed cellular actin dynamics.
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Publication type Article: Journal article
Document type Scientific Article
Keywords Different Structural States; F-actin; Barbed-end; Fluorescence Microscopy; Cofilin Increases; Adp-actin; Myosin; Cell; Elongation; Polymerization
Language english
Publication Year 2015
HGF-reported in Year 2015
ISSN (print) / ISBN 2050-084X
e-ISSN 2050-084X
Journal eLife
Quellenangaben Volume: 4 Issue: , Pages: , Article Number: , Supplement: ,
Publisher eLife Sciences Publications
Publishing Place Cambridge
Reviewing status Peer reviewed
Institute(s) Institute of Structural Biology (STB)
POF-Topic(s) 30203 - Molecular Targets and Therapies
Research field(s) Enabling and Novel Technologies
PSP Element(s) G-503000-001
PubMed ID 25706231
DOI 10.1101/008128
WOS ID WOS:000349821500001
Erfassungsdatum 2015-03-23
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