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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
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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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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 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).
In F-actin, the ADF/cofilin proteins...
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Introduction to Actin01:26

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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 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.
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Related Experiment Video

Updated: May 29, 2025

Dextran Labeling and Uptake in Live and Functional Murine Cochlear Hair Cells
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mTORC2 Regulates Actin Polymerization in Auditory Cells.

Michael Lanz1, Maurizio Cortada1,2, Yu Lu1

  • 1Department of Biomedicine, University of Basel, Basel, Switzerland.

Journal of Neurochemistry
|February 8, 2025
PubMed
Summary
This summary is machine-generated.

Mammalian target of rapamycin complex 2 (mTORC2) is crucial for hearing. mTORC2 deficiency in auditory cells disrupts the actin cytoskeleton and cell proliferation, offering insights into hearing loss.

Keywords:
HEI‐OC1Rictoractin cytoskeletonhair cellmTORC2

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Working with Auditory HEI-OC1 Cells
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Area of Science:

  • Cell Biology
  • Auditory Neuroscience
  • Molecular Biology

Background:

  • Mammalian target of rapamycin complex 2 (mTORC2) plays a vital role in hearing.
  • The precise mechanisms by which mTORC2 influences intracellular processes in auditory sensory hair cells remain unclear.

Purpose of the Study:

  • To investigate the mechanistic role of mTORC2 in auditory cell function.
  • To elucidate how mTORC2 regulates the actin cytoskeleton and proliferation in auditory cells.

Main Methods:

  • Generation of a Rictor knockout HEI-OC1 auditory cell line to create mTORC2-deficient cells.
  • Analysis of actin cytoskeleton morphology, cell proliferation rates, and protein phosphorylation.
  • Proteomic analysis to identify changes in protein expression.

Main Results:

  • mTORC2-deficient auditory cells showed significant alterations in actin cytoskeleton structure and reduced proliferation.
  • A decrease in protein kinase C alpha (PKCα) phosphorylation and impaired actin polymerization were observed.
  • Proteomics revealed altered expression of cytoskeleton-related proteins in mTORC2-disrupted cells.

Conclusions:

  • mTORC2 is essential for maintaining auditory cell structure and function, particularly the actin cytoskeleton.
  • These findings offer mechanistic insights into mTORC2's role in hearing.
  • This research may inform future therapeutic strategies for sensorineural hearing loss.