Requirements for contractility in disordered cytoskeletal bundles.
Martin Lenz1, Margaret L Gardel, Aaron R Dinner
1James Franck Institute, University of Chicago, Chicago, IL 60637, USA.
Summary
Contractile actomyosin bundles lacking muscle organization contract via non-identical motors and actin filament buckling. This mechanism explains force generation in simpler biological systems.
Area of Science:
- Biophysics
- Cell Biology
- Biochemistry
Background:
- Actomyosin contractility is crucial for biological force generation, particularly in organized muscle structures.
- Unorganized actomyosin bundles also exhibit contraction, defying conventional muscle models.
- Understanding these simpler systems offers insights into fundamental force-generating mechanisms.
Purpose of the Study:
- To investigate the microscopic symmetries governing contraction in disorganized actomyosin bundles.
- To identify the key molecular and mechanical factors driving contraction in these systems.
- To propose a mechanism for force generation beyond standard muscle theory.
Main Methods:
- Analysis of microscopic symmetries in actomyosin bundles.
- Theoretical modeling of motor-actin interactions.
- Investigation of F-actin's nonlinear elastic properties under motor-generated forces.
Main Results:
- Contractile behavior necessitates non-identical motors.
- Sufficiently large motor forces are required to engage nonlinear actin elasticity.
- Filament buckling emerges as a critical factor in bundle contraction.
Conclusions:
- Non-identical motors and actin filament buckling are key to unorganized actomyosin bundle contraction.
- This mechanism provides a framework for understanding force generation in simpler biological assemblies.
- Findings align with recent experimental observations in reconstituted actomyosin systems.
Related Concept Videos
The Role of Actin and Myosin in Non-muscle Cells
Actin and myosin or actomyosin filaments also play a significant role in cells other than those involved in muscle contraction (which occurs within the sarcomere of muscle cells). The mechanism of non-muscle cell contractile bundles was first observed in Dictyostelium and Acanthamoeba. In non-muscle cells, two bundles are commonly found: stress fibers and actomyosin adherence belts. These contractile bundles are smaller and less organized than the ones found in muscle cells. They are held...
Actin and Myosin in Muscle Contraction
Actin and myosin are contractile proteins that form the sarcomere found in skeletal muscle tissues for regulating muscle contraction. Actin, a globular contractile protein, interacts with myosin for muscle contraction. The skeletal tissue appears striped or striated under a microscope due to the repeated arrangement of contractile proteins actin and myosin along the length of myofibrils. Dark A bands and light I bands repeat along myofibrils, and the alignment of myofibrils in the cell causes...
The Contractile Ring
Contractile rings are composed of microfilaments and are responsible for separating the daughter cells during cytokinesis. Contractile ring assembly proceeds along with other cell cycle events; however, very few mechanistic details are known about the timing and coordination of the contractile rings with the cell cycle.
A small GTPase, RhoA, controls the function and assembly of the contractile ring. RhoA belongs to the Ras superfamily of proteins. The activation of formins by RhoA promotes...
A small GTPase, RhoA, controls the function and assembly of the contractile ring. RhoA belongs to the Ras superfamily of proteins. The activation of formins by RhoA promotes...
The Contractile Ring
Contractile rings are composed of microfilaments and are responsible for separating the daughter cells during cytokinesis. Contractile ring assembly proceeds along with other cell cycle events; however, very few mechanistic details are known about the timing and coordination of the contractile rings with the cell cycle.
A small GTPase, RhoA, controls the function and assembly of the contractile ring. RhoA belongs to the Ras superfamily of proteins. The activation of formins by RhoA promotes...
A small GTPase, RhoA, controls the function and assembly of the contractile ring. RhoA belongs to the Ras superfamily of proteins. The activation of formins by RhoA promotes...
Adaptability of Cytoskeletal Filaments
The cytoskeleton is a complex dynamic structure performing varied functions based on cellular requirements. The adaptability of the individual filaments in the cytoskeleton determines their ability to perform various functions within the cell. It can undergo rapid reorganization during processes like cell division or remain stable for several hours as in the interphase. The adaptability of these filaments depends on stringent regulatory mechanisms. The microfilament and microtubules of the...
Assembly of Cytoskeletal Filaments
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...

