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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...

Actin Polymerization

Actin 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...

Actin Polymerization and Cell Motility

Actin 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.

Cytoskeletal Accessory Proteins

Cytoskeletal Accessory Proteins

The cytoskeleton is an essential cell component that plays several structural and functional roles. However, the filaments that make up the cytoskeleton cannot function independently and depend on the accessory or ancillary proteins to effectively carry out their function. Accessory proteins associate with cytoskeletal filaments and their monomers, aiding filament formation and function. They also help in the cross-communication among cytoskeletal filaments. Cytoskeletal accessory proteins are...

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...

Mechanism of Filopodia Formation

Mechanism 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...

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Related Experiment Video

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Aip1p Dynamics Are Altered by the R256H Mutation in Actin

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p53-cofactor JMY is a multifunctional actin nucleation factor.

J Bradley Zuchero, Amanda S Coutts, Margot E Quinlan

Nature Cell Biology

|March 17, 2009

Summary

JMY protein nucleates actin filaments through Arp2/3 and Spire-like mechanisms, enhancing cell motility. Its nuclear sequestration regulates this multifunctional actin assembly factor.

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Area of Science:

Cell Biology
Biochemistry

Background:

Actin filament networks are crucial for cellular structures and their architecture depends on filament formation mechanisms.
Proteins like the Arp2/3 complex (branched networks) and Spire (unbranched filaments) are known actin nucleators.

Discussion:

JMY, a vertebrate protein, exhibits dual actin nucleation activity, activating Arp2/3 and directly assembling filaments via a Spire-like pathway.
JMY's expression levels correlate with cell motility; increased JMY enhances migration, while JMY loss impedes it.
Cellular localization of JMY shifts from the nucleus to the cytoplasm and leading edge during differentiation into motile neutrophil-like cells.

Key Insights:

JMY is a multifunctional actin assembly factor with both Arp2/3-activating and Spire-like nucleation capabilities.
JMY's activity is regulated by its subcellular localization, with nuclear sequestration playing a role in controlling its function.
JMY plays a significant role in regulating cell migration and motility.

Outlook:

Further investigation into JMY's transcriptional co-activator role and its interplay with actin nucleation.
Exploring the precise molecular mechanisms of JMY's Spire-like filament assembly.
Investigating JMY's regulation in various cell types and physiological processes beyond migration.