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Related Concept Videos

Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

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...
SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
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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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Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
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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.
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Updated: May 17, 2026

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
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Published on: January 11, 2017

Structural insights into dynamin-mediated membrane fission.

Katja Faelber1, Martin Held, Song Gao

  • 1Max-Delbrück-Centrum for Molecular Medicine, Crystallography, Robert-Rössle-Strasse 10, 13125 Berlin, Germany. katja.faelber@mdc-berlin.de

Structure (London, England : 1993)
|October 16, 2012
PubMed
Summary
This summary is machine-generated.

Dynamin, a protein crucial for cell membrane scission, forms helical filaments. This review details its structure and proposes a model for how dynamin

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • Dynamin is a key mechanochemical GTPase regulating membrane scission.
  • Its function is particularly critical in clathrin-coated vesicle endocytosis.
  • Recent studies have illuminated the structural basis of dynamin filament assembly.

Purpose of the Study:

  • To review recent structural and mechanistic insights into dynamin.
  • To discuss the inherent architecture of dynamin that facilitates helical filament formation.
  • To propose a structure-based model for dynamin-mediated membrane scission.

Main Methods:

  • Review of existing structural and mechanistic data on dynamin.
  • Analysis of dynamin domain interactions during filament assembly.
  • Integration of findings to propose a novel model.

Main Results:

  • Dynamin self-assembles into helical filaments through dynamic domain interactions.
  • Nucleotide binding triggers large-scale conformational changes essential for scission.
  • The protein's architecture is inherently suited for right-handed helical filament formation.

Conclusions:

  • Dynamin's structure dictates its assembly into functional helical filaments.
  • A proposed structure-based model explains dynamin's role in membrane scission.
  • Understanding dynamin structure-function relationships is key to deciphering endocytic mechanisms.