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Actin filament elasticity and retrograde flow shape the force-velocity relation of motile cells.


ABSTRACT: Cells migrate through a crowded environment during processes such as metastasis or wound healing, and must generate and withstand substantial forces. The cellular motility responses to environmental forces are represented by their force-velocity relation, which has been measured for fish keratocytes but remains unexplained. Even pN opposing forces slow down lamellipodium motion by three orders of magnitude. At larger opposing forces, the retrograde flow of the actin network accelerates until it compensates for polymerization, and cell motion stalls. Subsequently, the lamellipodium adapts to the stalled state. We present a mechanism quantitatively explaining the cell's force-velocity relation and its changes upon application of drugs that hinder actin polymerization or actomyosin-based contractility. Elastic properties of filaments, close to the lamellipodium leading edge, and retrograde flow shape the force-velocity relation. To our knowledge, our results shed new light on how these migratory responses are regulated, and on the mechanics and structure of the lamellipodium.

SUBMITTER: Zimmermann J 

PROVIDER: S-EPMC3260663 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature

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Actin filament elasticity and retrograde flow shape the force-velocity relation of motile cells.

Zimmermann Juliane J   Brunner Claudia C   Enculescu Mihaela M   Goegler Michael M   Ehrlicher Allen A   Käs Josef J   Falcke Martin M  

Biophysical journal 20120101 2


Cells migrate through a crowded environment during processes such as metastasis or wound healing, and must generate and withstand substantial forces. The cellular motility responses to environmental forces are represented by their force-velocity relation, which has been measured for fish keratocytes but remains unexplained. Even pN opposing forces slow down lamellipodium motion by three orders of magnitude. At larger opposing forces, the retrograde flow of the actin network accelerates until it  ...[more]

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