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Related Concept Videos

Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

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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.
Membrane bending can happen due to intrinsic changes in lipid composition or extrinsic association with different proteins. The proteins involved...
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Mechanisms of Membrane Domain Formation00:59

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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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Membrane Fluidity01:26

Membrane Fluidity

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Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
Mosaic nature of the membrane
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is...
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Membrane Fluidity01:23

Membrane Fluidity

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Cell membranes are composed of phospholipids, proteins, and carbohydrates loosely attached to one another through chemical interactions. Molecules are generally able to move about in the plane of the membrane, giving the membrane its flexible nature called fluidity. Two other features of the membrane contribute to membrane fluidity: the chemical structure of the phospholipids and the presence of cholesterol in the membrane.
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Cooperative Allosteric Transitions01:58

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Cooperative Allosteric Transitions01:58

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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Updated: Feb 27, 2026

Neutron Spin Echo Spectroscopy as a Unique Probe for Lipid Membrane Dynamics and Membrane-Protein Interactions
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MinE conformational dynamics regulate membrane binding, MinD interaction, and Min oscillation.

Kyung-Tae Park1, Maria T Villar2, Antonio Artigues2

  • 1Department of Microbiology, Molecular Genetics & Immunology, University of Kansas Medical Center, Kansas City, KS 66160.

Proceedings of the National Academy of Sciences of the United States of America
|June 28, 2017
PubMed
Summary
This summary is machine-generated.

MinE protein dynamics in Escherichia coli are crucial for cell division. Its conformational switch, regulated by membrane targeting sequences, ensures proper Z-ring placement, revealing mechanisms of MinE activation and ring formation.

Keywords:
Min oscillatorMinDMinEconformational dynamicsself-organization

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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
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In Vitro Reconstitution of Self-Organizing Protein Patterns on Supported Lipid Bilayers
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Area of Science:

  • Bacterial cell division
  • Protein conformational dynamics
  • Cytoskeletal regulation

Background:

  • MinE protein in Escherichia coli orchestrates cell division by inducing MinC/MinD oscillations.
  • Accurate Z-ring placement at midcell relies on MinE's conformational change from a latent cytoplasmic form to an active membrane-bound form.
  • The mechanism governing MinE's conformational switch and activation remains largely unknown.

Purpose of the Study:

  • To investigate the mechanism of MinE conformational change during Escherichia coli cell division.
  • To elucidate the role of MinE's dynamic structure in its interaction with MinD and membrane localization.
  • To understand the regulation of MinE activation and MinE ring formation.

Main Methods:

  • Hydrogen-deuterium exchange coupled to mass spectrometry (HDX-MS) was employed to study MinE dynamics.
  • Analysis of a MinE mutant (D45A/V49A) with aberrant oscillation and ring formation defects.
  • Investigation of intragenic suppressors to identify genetic elements affecting MinE function.

Main Results:

  • HDX-MS ruled out a rapid equilibrium model for MinE's latent and active forms.
  • The MinE mutant (D45A/V49A) exhibited increased rigidity and impaired interaction with MinD, indicating a defect in switching to the active form.
  • Analysis suggested the mutant struggles to release its N-terminal membrane targeting sequences (MTS).

Conclusions:

  • MinE's conformational switch is not a rapid equilibrium but a regulated process.
  • The dynamic association of MTS with MinE's β-sheet is critical for balancing cytoplasmic diffusion and membrane sensing.
  • These findings provide insights into MinE activation and the formation of the MinE ring essential for bacterial cytokinesis.