An active biopolymer network controlled by molecular motors.
basic_science · Level V
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- Record sourced from PubMed, PMID 19667200.
- Also identified by DOI 10.1073/pnas.0903974106 and PMC identifier 2741227.
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Abstract
We describe an active polymer network in which processive molecular motors control network elasticity. This system consists of actin filaments cross-linked by filamin A (FLNa) and contracted by bipolar filaments of muscle myosin II. The myosin motors stiffen the network by more than two orders of magnitude by pulling on actin filaments anchored in the network by FLNa cross-links, thereby generating internal stress. The stiffening response closely mimics the effects of external stress applied by mechanical shear. Both internal and external stresses can drive the network into a highly nonlinear, stiffened regime. The active stress reaches values that are equivalent to an external stress of 14 Pa, consistent with a 1-pN force per myosin head. This active network mimics many mechanical properties of cells and suggests that adherent cells exert mechanical control by operating in a nonlinear regime where cell stiffness is sensitive to changes in motor activity. This design principle may be applicable to engineering novel biologically inspired, active materials that adjust their own stiffness by internal catalytic control.
Medical subject headings
- Actins
- Biomedical Engineering
- Contractile Proteins
- Cytoskeleton
- Microfilament Proteins
- Molecular Motor Proteins
- Polymers