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Updated: May 11, 2026
08:02
Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
Published on: May 5, 2022
Tension modulates actin filament polymerization mediated by formin and profilin
Naomi Courtemanche1, Ja Yil Lee, Thomas D Pollard
1Departments of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520-8103, USA. thomas.pollard@yale.edu
Summary
Tension significantly impacts actin filament assembly by formins. Forces slow polymerization without profilin but accelerate it with profilin, revealing a tension-dependent mechanism for actin dynamics.
Area of Science:
- Cell Biology
- Biochemistry
- Biophysics
Background:
- Formins are crucial proteins that regulate actin filament elongation for cellular structures like contractile rings.
- Cellular structures are often under physical tension, but its effect on formin-mediated actin assembly was not understood.
Purpose of the Study:
- To investigate how physical tension affects actin polymerization mediated by the yeast formin Bni1p at the single-molecule level.
Main Methods:
- Utilized single-molecule imaging techniques to observe actin polymerization dynamics.
- Applied controlled forces to actin filaments during formin-mediated elongation.
Main Results:
- Applied forces significantly slowed actin polymerization by Bni1p in the absence of profilin.
- In the presence of profilin, applied forces led to accelerated actin polymerization.
- Proposed a model where force shifts the conformational equilibrium of formin domains, modulated by profilin-actin interactions.
Conclusions:
- Physical forces play a critical role in regulating formin-mediated actin assembly.
- Profilin acts as a key modulator, reversing the inhibitory effects of tension on actin polymerization.
- These findings provide new insights into the mechanical regulation of the actin cytoskeleton.
Related Concept Videos
01:14Generation of Straight or Branched Actin Filaments
The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
01:42Actin Polymerization
Actin polymerization occurs through the head-to-tail association of binding sites on monomeric actin or G-actin to form filamentous or F-actin. The polymerization can be divided into three phases ̶ nucleation, elongation, and steady-state phase.
The nucleation phase involves forming a stable nucleus consisting of three actin monomers to form a new actin filament. Actin-binding proteins such as formins and Arp2/3 complex help filament growth post-nucleation. The Formins form straight actin...
The nucleation phase involves forming a stable nucleus consisting of three actin monomers to form a new actin filament. Actin-binding proteins such as formins and Arp2/3 complex help filament growth post-nucleation. The Formins form straight actin...
01:11Formation of Higher-order Actin Filaments
The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin networks...
The high-order actin networks...
01:19Actin Filament Depolymerization
Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...
In F-actin, the ADF/cofilin proteins...
01:39Mechanism of Filopodia Formation
Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
01:13Actin Polymerization and Cell Motility
Actin is a family of globular proteins that are highly abundant in eukaryotic cells. It makes up approximately 1-5% of total cell protein concentration. Actin monomers polymerize to form a complex network of polarized filaments, the actin cytoskeleton, that plays a crucial role in many cellular processes, including cell motility, division, endocytosis, and metastasis of cancer cells.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate.