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The Contractile Ring

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...

The Contractile Ring

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...

Pinching-off of Coated Vesicles

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...

Generation of Straight or Branched Actin Filaments

Generation 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...

Disassembly of Intermediate Filaments

Disassembly of Intermediate Filaments

Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...

Actin Filament Depolymerization

Actin 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...

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Related Experiment Video

Updated: May 8, 2026

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro

Published on: January 11, 2017

Dynamin rings: not just for fission.

Sanja Sever¹, Joann Chang, Changkyu Gu

¹Nephrology Division, Massachusetts General Hospital, CNY 149 8.113, 149 13th Street, Charlestown, MA, 02129, USA.

Traffic (Copenhagen, Denmark)

|August 29, 2013

Summary

GTPase dynamin

Area of Science:

Biochemistry and Cell Biology

Background:

Dynamin is a GTPase crucial for cellular processes like endocytosis and actin cytoskeleton regulation.
Its oligomerization into higher-order structures is key to vesicle formation and actin dynamics.

Purpose of the Study:

To explore the molecular mechanisms underlying dynamin's role in actin cytoskeleton regulation.
To investigate the novel functions of dynamin oligomerization in cellular processes.

Main Methods:

Biochemical assays to study dynamin's properties.
Cellular imaging to observe dynamin's localization and function.
Genetic manipulation to probe dynamin's interactions with actin-binding proteins.

Main Results:

Dynamin oligomerization plays a significant role in regulating actin polymerization.

Keywords:

dynamin actin endocytosis microtubules oligomerization

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New insights reveal dynamin's involvement beyond endocytosis, particularly in actin dynamics.

The study elucidates molecular mechanisms of dynamin's action on the actin cytoskeleton.

Conclusions:

Dynamin's function extends beyond endocytosis, highlighting its critical role in actin regulation.
Dynamin oligomerization represents a novel mechanism for controlling actin polymerization.
Further research into dynamin's multifaceted roles is warranted for a comprehensive understanding of cellular dynamics.