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Related Concept Videos

Actin Polymerization01:42

Actin Polymerization

7.1K
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 Treadmilling01:18

Actin Treadmilling

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Actin filaments undergo polymerization and depolymerization from either end. The polymerization and depolymerization rates depend on the cytosolic concentration of free G-actins. The polymerization rate is generally higher at the plus or barbed end, while the depolymerization rate is higher at the minus or pointed end. At a steady state, critical concentration describes the concentration of free G-actin monomers at which the polymerization rate at the plus end is equal to that of the...
8.3K
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

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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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Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

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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....
5.6K
Actin Filament Depolymerization01:19

Actin Filament Depolymerization

3.3K
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...
3.3K
Mechanism of Lamellipodia Formation01:31

Mechanism of Lamellipodia Formation

2.8K
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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Related Experiment Video

Updated: Sep 30, 2025

A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues
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A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues

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Parallel kinase pathways stimulate actin polymerization at depolarized mitochondria.

Tak Shun Fung1, Rajarshi Chakrabarti1, Jana Kollasser2

  • 1Department of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth College, Hanover, NH 03755, USA.

Current Biology : CB
|March 15, 2022
PubMed
Summary
This summary is machine-generated.

Acute damage-induced actin (ADA) polymerization around mitochondria is triggered by two signaling pathways, involving calcium and ATP changes. This actin network prevents rapid mitochondrial shape changes.

Keywords:
AMPKArp2/3 complexCCCPFMNL forminsOMA1OPA1PKCβactincalciummitochondrial depolarization

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In Vitro Polymerization of F-actin on Early Endosomes
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In Vitro Polymerization of F-actin on Early Endosomes

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Related Experiment Videos

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A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues
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Time-Lapse Video Microscopy for Assessment of EYFP-Parkin Aggregation as a Marker for Cellular Mitophagy
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In Vitro Polymerization of F-actin on Early Endosomes
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In Vitro Polymerization of F-actin on Early Endosomes

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Area of Science:

  • Cell Biology
  • Mitochondrial Biology
  • Actin Dynamics

Background:

  • Mitochondrial damage (MtD) disrupts cellular homeostasis, triggering metabolic shifts and mitophagy.
  • Acute damage-induced actin (ADA) is a rapid actin polymerization response to MtD, but its activation mechanism is unclear.

Purpose of the Study:

  • To elucidate the signaling pathways and molecular mechanisms regulating ADA formation upon mitochondrial damage.
  • To investigate the functional role of ADA in response to mitochondrial depolarization.

Main Methods:

  • Induction of ADA using mitochondrial depolarization or metformin.
  • Analysis of signaling pathways involving calcium, ATP, PKC-β, AMPK, Rac, Cdc42, Arp2/3 complex, and FMNL formins.
  • Identification and functional assessment of guanine nucleotide exchange factors Trio and Fgd1.
  • Investigation of mitochondrial calcium dynamics via NCLX.
  • Assessment of mitochondrial shape changes and Opa1 processing upon ADA inhibition.

Main Results:

  • Two parallel pathways activate ADA: one via calcium/PKC-β/Rac/Arp2/3, the other via ATP drop/AMPK/Cdc42/formin.
  • Trio and Fgd1 act as guanine nucleotide exchange factors for Rac and Cdc42, respectively, and are crucial for ADA.
  • Mitochondrial calcium efflux via NCLX initiates the calcium-dependent pathway.
  • ADA network formation inhibits rapid mitochondrial inner membrane circularization, dependent on Oma1 and Opa1 processing.

Conclusions:

  • ADA formation requires coordinated action of Arp2/3 complex and formins, regulated by distinct calcium and ATP-dependent signaling cascades.
  • The ADA actin network serves a protective role by preventing detrimental mitochondrial shape alterations during stress.