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Related Concept Videos

Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
Membrane bending can happen due to intrinsic changes in lipid composition or extrinsic association with different proteins. The proteins involved...
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Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
Mechanism of Filopodia Formation01:39

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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.
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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...
Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

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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A migrating cell changes its shape during the cyclic events of attachment and detachment from the substratum and repositions the cell organelles correspondingly. These complex events are orchestrated by the dynamic cytoskeletal network comprising actin filaments, intermediate filaments, and microtubules. Cytoskeletal crosstalk — the direct and indirect communication between the different components — is crucial for this coordination. Direct communication involves various linker proteins that...

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Pulling Membrane Nanotubes from Giant Unilamellar Vesicles
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Published on: December 7, 2017

Membrane curvature controls dynamin polymerization.

Aurélien Roux1, Gerbrand Koster, Martin Lenz

  • 1Physico-Chimie Curie, Institut Curie, Centre de Recherche, Unité Mixte de Recherche 168, Centre National de la Recherche Scientifique, Université Pierre et Marie Curie, F-75248 Paris, France. aurelien.roux@curie.fr

Proceedings of the National Academy of Sciences of the United States of America
|February 18, 2010
PubMed
Summary
This summary is machine-generated.

Dynamin proteins generate force to deform membranes, but high tension can resist this. At low concentrations, dynamin recruitment to membrane buds depends on curvature, guiding protein assembly.

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Area of Science:

  • Cell Biology
  • Biophysics

Background:

  • Membrane curvature generation is crucial for intracellular traffic.
  • Dynamin-like proteins deform lipid bilayers and drive membrane fission.
  • Dynamin polymerization into a helical coat is hypothesized to cause membrane deformation.

Purpose of the Study:

  • To investigate the force generated by dynamin polymerization.
  • To determine the role of membrane curvature in dynamin recruitment.
  • To understand the mechanism of dynamin-mediated membrane deformation and fission.

Main Methods:

  • Experimental measurement of force generated by dynamin polymerization.
  • Observation of dynamin nucleation dependence on membrane curvature at varying concentrations.
  • Theoretical modeling of dynamin polymerization and membrane mechanics.

Main Results:

  • Dynamin polymerization generates 18 pN force, sufficient for membrane deformation but counteracted by high membrane tension.
  • At low dynamin concentrations, polymer nucleation is highly dependent on membrane curvature.
  • This curvature dependence suggests specific recruitment of dynamin to highly curved membrane bud necks.

Conclusions:

  • Dynamin's force generation is key to membrane deformation, but membrane tension modulates this process.
  • Curvature-dependent recruitment provides a mechanism for precise dynamin localization to membrane bud necks.
  • The findings offer a generalizable model for curvature-coupled protein assembly on membranes.