Related Experiment Video
Updated: Nov 24, 2025

08:57
Aip1p Dynamics Are Altered by the R256H Mutation in Actin
Published on: July 30, 2014
8.2K
Bioinformatics Analysis of Actin Molecules: Why Quantity Does Not Translate Into Quality?
Anna V Glyakina1,2, Oxana V Galzitskaya1,3
1Institute of Protein Research, Russian Academy of Sciences, Pushchino, Russia.
Frontiers in Genetics
|December 28, 2020
Summary
Actin
Area of Science:
- Biochemistry
- Structural Biology
- Bioinformatics
Background:
- Filamentous actin's double-stranded organization doesn't explain its polymorphism.
- Actin is a crucial molecule in cellular processes.
- Understanding actin's structure is key to its function.
Purpose of the Study:
- To identify distinctive characteristics of actin.
- To analyze the conservatism of actin's primary structure in Chordata.
- To investigate actin's structural features using bioinformatics and structural data.
Main Methods:
- Bioinformatics analysis of 296 Chordate actin amino acid sequences.
- Analysis of 155 rabbit actin structures from X-ray diffraction and electron microscopy.
- Pairwise alignment and root-mean-square deviation (RMSD) calculations.
Main Results:
- Determined the degree of primary structure conservatism in Chordate actin.
- Found high similarity among 155 rabbit actin structures (RMSD < 3 Å).
- Identified unusual internal localization of charged residues and linked exon regions to structural subdomains.
Conclusions:
- Existing models of double-stranded actin organization may be insufficient.
- New approaches are needed to test actin's double-stranded organization.
- Structural analysis reveals novel insights into actin's unique characteristics.
Related Concept Videos
Introduction to Actin
5.9K
Actin is a highly conserved cytoskeletal protein found abundantly in eukaryotic cells. It constitutes 10% weight of the total cellular protein in muscle cells, while in non-muscle cells, it is lower and makes up around 1–5 percent of the total cell protein. Actin found in the unicellular amoebae and complex multicellular animals is around 80% similar, demonstrating their conservation over a billion years of evolution. Actin coding genes are conserved within species and across...
5.9K
Actin Polymerization and Cell Motility
6.1K
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....
6.1K
Actin Polymerization
7.8K
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...
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...
7.8K
Generation of Straight or Branched Actin Filaments
3.5K
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...
3.5K
Formation of Higher-order Actin Filaments
3.3K
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...
The high-order actin...
3.3K
Actin Filament Depolymerization
3.5K
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...
3.5K

