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Related Concept Videos

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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Actin Polymerization01:42

Actin Polymerization

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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...
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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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Mechanism of Lamellipodia Formation01:31

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Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
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Anaphase Promoting Complex00:50

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The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
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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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Related Experiment Video

Updated: Dec 7, 2025

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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Aip1p Dynamics Are Altered by the R256H Mutation in Actin

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EB1 Directly Regulates APC-Mediated Actin Nucleation.

Maria Angeles Juanes1, Colby P Fees2, Gregory J Hoeprich2

  • 1Biology Department, Brandeis University, 415 South Street, Waltham, MA 02454, USA; School of Health and Life Science, Teesside University, Middlesbrough TS1 3BX, UK; National Horizons Centre, Teesside University, 38 John Dixon Lane, Darlington DL1 1HG, UK.

Current Biology : CB
|October 2, 2020
PubMed
Summary

EB1 protein binds to the adenomatous polyposis coli protein (APC) and inhibits its actin nucleation function. This discovery reveals a new role for EB1 in regulating cell migration and cytoskeletal dynamics.

Keywords:
APCEB1TIRF microscopyactincell migrationfocal adhesionmicrotubules

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Labeling F-actin Barbed Ends with Rhodamine-actin in Permeabilized Neuronal Growth Cones
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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • EB1 is a microtubule end-tracking protein (+TIP) and a known binding partner of APC.
  • APC's C-terminal basic domain (APC-B) nucleates actin assembly, crucial for cell migration and F-actin levels.
  • The functional significance of EB1-APC interactions beyond microtubule regulation is not well understood.

Purpose of the Study:

  • To investigate whether EB1 interactions regulate APC functions beyond microtubule dynamics.
  • To elucidate the role of EB1 in modulating APC-mediated actin nucleation.

Main Methods:

  • Biochemical assays to test EB1 binding to APC-B.
  • Cell-based experiments involving EB1 knockdown and overexpression.
  • Assessment of F-actin levels and cell migration assays.

Main Results:

  • EB1 directly binds to APC-B and inhibits its actin nucleation activity by blocking actin monomer recruitment.
  • EB1 knockdown increases F-actin levels, while EB1 overexpression decreases F-actin levels and impairs directed cell migration.
  • These effects on F-actin and cell migration are independent of EB1's interaction with microtubules.

Conclusions:

  • EB1 negatively regulates APC-mediated actin assembly, defining a novel function for EB1.
  • EB1-APC interactions coordinate microtubule and actin dynamics, suggesting a role in bidirectional cytoskeletal crosstalk.