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Related Concept Videos

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

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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).
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Actin Treadmilling01:18

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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...
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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.
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Anaphase A and B01:39

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Microtubules form through the end-to-end polymerization of tubulin heterodimers. Kinetochore microtubules originate from the spindle poles, and their plus-ends connect with the kinetochores on sister-chromatids. Ndc80 protein complexes, present on the kinetochore, form low-affinity links with the plus end of these kinetochore microtubules.
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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
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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
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Accelerated actin filament polymerization from microtubule plus ends.

Jessica L Henty-Ridilla1, Aneliya Rankova1, Julian A Eskin1

  • 1Department of Biology, Brandeis University, 415 South Street, Waltham, MA 02454, USA.

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Summary

Microtubules (MTs) direct actin assembly through CLIP-170 binding to formins. This interaction accelerates actin polymerization and influences neuronal structure.

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Area of Science:

  • Cell Biology
  • Cytoskeletal Dynamics
  • Molecular Motors

Background:

  • Microtubules (MTs) and actin filaments are key cytoskeletal components involved in numerous cellular processes.
  • The precise mechanisms of cross-talk and coordination between MTs and actin networks remain largely unknown.
  • Understanding cytoskeletal interactions is crucial for comprehending cell structure, migration, and division.

Purpose of the Study:

  • To elucidate the molecular mechanisms by which microtubules regulate actin network remodeling.
  • To investigate the role of the microtubule-associated protein CLIP-170 in mediating cytoskeletal cross-talk.
  • To determine how microtubule dynamics influence actin filament assembly and cellular morphology.

Main Methods:

  • Single-molecule fluorescence microscopy to observe protein interactions and dynamics.
  • In vitro reconstitution assays to study microtubule-actin dynamics.
  • Co-observation of microtubule and actin filament growth in a reconstituted system.
  • Analysis of dendritic morphology in primary neurons.

Main Results:

  • CLIP-170 directly binds to formins, accelerating actin filament elongation.
  • CLIP-170-formin complexes (specifically mDia1) form stable dimers that cotrack growing filament ends.
  • These complexes enhance actin polymerization rates approximately 18-fold and protect filaments from capping proteins.
  • EB1 recruits CLIP-170-formin complexes to growing microtubule plus-ends, initiating rapid, MT-associated actin assembly.
  • CLIP-170 function is essential for normal dendritic morphology in primary neurons.

Conclusions:

  • Growing microtubule plus-ends serve as platforms to direct rapid actin assembly via CLIP-170 and formin interactions.
  • This mechanism provides a direct link between microtubule dynamics and actin network organization.
  • The findings reveal a novel pathway for cytoskeletal coordination with implications for neuronal development and function.