Related Experiment Video

Updated: Aug 18, 2026

Measuring Protein Binding to F-actin by Co-sedimentation
06:17

Measuring Protein Binding to F-actin by Co-sedimentation

Published on: May 18, 2017

Fyn binding protein, Fyb, interacts with mammalian actin binding protein, mAbp1

Ming Yuan1, Lena Mogemark, Maria Fällman

  • 1Department of Molecular Biology, Umeå University, Sweden.

FEBS Letters
|April 26, 2005
PubMed

Insights

We discovered that mammalian actin binding protein 1 (mAbp1) interacts with Fyn-T binding protein (Fyb) in macrophages. This interaction is crucial for regulating F-actin dynamics, suggesting a new role for mAbp1 in immune cell function.

Area of Science:

  • Immunology
  • Cell Biology
  • Protein Interactions

Background:

  • Fyn-T binding protein (Fyb) is an immune cell protein targeted by Yersinia outer protein H (YopH).
  • The specific function of Fyb within macrophages remains largely uncharacterized.

Purpose of the Study:

  • To identify novel interaction partners of Fyb in macrophages.
  • To elucidate the functional role of Fyb and its interacting proteins in macrophage biology.

Main Methods:

  • A mouse lymphoma cDNA library was screened using Fyb domains as bait.
  • Co-localization studies with F-actin were performed in macrophage lysates.

Main Results:

  • Mammalian actin binding protein 1 (mAbp1) was identified as a novel Fyb-interacting protein.
  • mAbp1 binds to the N-terminus of Fyb via its C-terminal src homology 3 domain.
  • Both Fyb and mAbp1 were found to co-localize with F-actin at the leading edge of macrophages.

Conclusions:

  • Mammalian actin binding protein 1 (mAbp1) is a novel downstream effector of Fyb.
  • The Fyb-mAbp1 complex likely plays a significant role in regulating F-actin dynamics in macrophages.

More Related Videos

Aip1p Dynamics Are Altered by the R256H Mutation in Actin08:57

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Published on: July 30, 2014

Methods to Study Mrp4-containing Macromolecular Complexes in the Regulation of Fibroblast Migration10:43

Methods to Study Mrp4-containing Macromolecular Complexes in the Regulation of Fibroblast Migration

Published on: May 19, 2016

Related Concept Videos

Generation of Straight or Branched Actin Filaments01:14

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

Formation 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...
Actin Filament Depolymerization01:19

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 Polymerization01:42

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...
Cytoskeletal Accessory Proteins01:13

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...
Introduction to Actin01:26

Introduction to Actin

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 different species.