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Related Concept Videos

Introduction to Actin01:26

Introduction to Actin

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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...
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Actin Polymerization and Cell Motility01:13

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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....
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Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

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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...
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Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

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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...
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Actin Filament Depolymerization01:19

Actin Filament Depolymerization

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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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Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

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Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
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Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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On the Interaction Between Human IQGAP1 and Actin.

Damian J Magill, Elaine Hamilton, Sally L Shirran

  • 1School of Pharmacy and Biomolecular Sciences, University of Brighton, Huxley Building, Lewes Road, Brighton BN2 4GJ. UK. d.timson@brighton.ac.uk.

Protein and Peptide Letters
|February 5, 2016
PubMed
Summary
This summary is machine-generated.

The calponin homology domain of IQGAP1 binds alpha-actin via an electrostatic interaction. This interaction, conserved across eukaryotes, may initiate complex formation between IQGAP1-like proteins and their partners.

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Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin
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Quantification of Filamentous Actin F-actin Puncta in Rat Cortical Neurons
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Area of Science:

  • Cellular biology
  • Biochemistry
  • Structural biology

Background:

  • IQGAP proteins act as crucial signaling hubs, relaying external signals to the cytoskeleton.
  • Understanding IQGAP1 protein interactions is key to deciphering its cellular functions.
  • Specific protein-interface knowledge is needed to elucidate IQGAP1's signaling mechanisms.

Purpose of the Study:

  • To investigate the interaction between the calponin homology domain of human IQGAP1 (CHD1) and alpha-actin.
  • To characterize the binding interface and stoichiometry of the CHD1-alpha-actin complex.
  • To predict the evolutionary conservation and functional implications of this interaction.

Main Methods:

  • Biochemical crosslinking to identify interacting protein regions.
  • Molecular modeling to build a complex structure.
  • Bioinformatics analysis to predict binding residues and conservation.

Main Results:

  • Human IQGAP1's calponin homology domain (CHD1) directly crosslinks with alpha-actin in a 1:1 stoichiometry.
  • Molecular modeling identified a specific electrostatic interaction between Lys-240 of alpha-actin and Glu-30 of CHD1.
  • This binding interface is evolutionarily conserved in IQGAP-like proteins, often in flexible, disordered regions.

Conclusions:

  • The identified electrostatic interaction is likely the initial binding event between CHD1 and alpha-actin.
  • This conserved interaction mechanism suggests a fundamental role in IQGAP1-like protein complex formation.
  • Subsequent conformational changes may refine the final complex structure.