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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 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.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate....
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Introduction to Membrane Proteins01:16

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The cell membrane, or plasma membrane, is an ever-changing landscape. It is described as a fluid mosaic where various macromolecules are embedded in the phospholipid bilayer. Among the macromolecules are proteins. The protein content varies across cell types. For example, mitochondrial inner membranes contain ~76% protein content, while myelin contains ~18% protein content. Individual cells contain many types of membrane proteins—red blood cells contain over 50—and different cell...
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Membrane Lipids01:32

Membrane Lipids

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Lipids are an essential component of all biological membranes. The average lipid content in mammalian membranes is 50%, though it can be as low as 20% in the inner mitochondrial membrane or as high as 80% in the myelin sheath present around the nerve cells.
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Membrane Proteins

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Plasma membranes have integral transmembrane proteins involved in facilitated transport. These proteins are collectively referred to as transport proteins, and they function as either channels for the material or as carriers themselves. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids and a hydrophilic channel through their core that provides a hydrated opening for solutes to pass through the membrane layers. Passage through the channel allows...
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Reconstitution of Membrane-Tethered Minimal Actin Cortices on Supported Lipid Bilayers
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Capping protein-controlled actin polymerization shapes lipid membranes.

Katharina Dürre1, Felix C Keber1,2, Philip Bleicher1

  • 1Lehrstuhl für Zellbiophysik, Technische Universität München, James-Franck-Str. 1, D-85748, Garching, Germany.

Nature Communications
|April 26, 2018
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Capping protein concentration controls actin-driven membrane shape changes. High concentrations promote inward bending, while low concentrations favor outward protrusions, revealing key cytoskeletal regulation mechanisms.

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Area of Science:

  • Cell biology
  • Biophysics
  • Cytoskeletal dynamics

Background:

  • The Arp2/3 complex drives actin assembly at cell membranes, crucial for forming protrusions and endocytic vesicles.
  • Understanding the precise mechanisms governing diverse membrane deformations remains a key challenge in cell biology.

Purpose of the Study:

  • To reconstitute and investigate the fundamental modes of membrane deformation (inward and outward bending) driven by cytoskeletal proteins in a controlled system.
  • To elucidate the role of capping protein (CP) concentration in regulating membrane shape and actin assembly dynamics.

Main Methods:

  • Reconstitution of minimal cytoskeletal protein systems within giant unilamellar vesicles (GUVs) to mimic confined cellular geometries.
  • Systematic variation of capping protein (CP) concentrations to observe effects on membrane deformation.
  • Addition of non-muscle myosin II to assess its impact on vesicle dynamics.
  • Computational simulations to rationalize observed deformation modes based on reaction kinetics.

Main Results:

  • Low capping protein (CP) concentrations favor the formation of membrane protrusions (outward bending).
  • High CP concentrations promote the formation of negatively bent membrane domains (inward bending).
  • Non-muscle myosin II addition induces complete membrane fission events within the reconstituted system.
  • Simulations correlate observed membrane deformations with the transient kinetics of the protein system.

Conclusions:

  • Capping protein concentration is a critical regulator of Arp2/3 complex-mediated membrane deformation, controlling the balance between outward and inward bending.
  • The study highlights the importance of quantitative understanding of microscopic kinetic balances for deciphering cytoskeletal functions.
  • Experimental validation in mouse melanoma cells supports the relevance of CP concentration in regulating cytoskeletal-driven membrane dynamics.