Modeling Pulling Force Generation by Ensembles of Polymerizing Actin Filaments
نویسندگان
چکیده
منابع مشابه
Effects of Hydrolysis on Force Generation by Actin Filaments
The effects of ATP hydrolysis on actin polymerization-based force generation are calculated using a multistate two-state Brownian-ratchet model based on measured polymerization curves. For ensembles of filaments pushing against a rigid obstacle, the stall force per filament can be much less than the equilibrium ATP-actin stall force. PACS numbers: 87.15.Rn,87.17.Jj,87.16.Ac,87.15.Cc
متن کاملForce generation by actin polymerization II: the elastic ratchet and tethered filaments.
The motion of many intracellular pathogens is driven by the polymerization of actin filaments. The propulsive force developed by the polymerization process is thought to arise from the thermal motions of the polymerizing filament tips. Recent experiments suggest that the nucleation of actin filaments involves a phase when the filaments are attached to the pathogen surface by a protein complex. ...
متن کاملStochastic force generation by small ensembles of myosin II motors.
Forces in the actin cytoskeleton are generated by small groups of nonprocessive myosin II motors for which stochastic effects are highly relevant. Using a cross-bridge model with the assumptions of fast power-stroke kinetics and equal load sharing between equivalent states, we derive a one-step master equation for the activity of a finite-sized ensemble of mechanically coupled myosin II motors....
متن کاملOn the length distribution in bundles of polymerizing and depolymerizing actin filaments
A model for the dynamics of the length distribution in polymer bundles is presented. It considers nucleation, polymerization, and depolymerization and is derived as a continuous macroscopic limit from a discrete description. Its main feature is a nonlinear coupling due to competition of the depolymerizing ends for the limited supply of a depolymerization agent. The model takes the form of an in...
متن کاملForce generation by Myosin II Filaments in Compliant Networks
Myosin II isoforms with varying mechanochemistry and filament size interact with filamentous actin (F-actin) networks to generate contractile forces in muscle and non-muscle cells. How their properties control force production in environments with varying stiffness remains poorly understood. Here, we incorporated literature values for biophysical properties of myosin II isoforms into a cross-br...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2018
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2017.11.806