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Related Concept Videos

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...
Fluid Mosaic Model01:19

Fluid Mosaic Model

Scientists identified the plasma membrane in the 1890s and its principal chemical components (lipids and proteins) by 1915. The model for plasma membrane structure, proposed in 1935 by Hugh Davson and James Danielli, was the first model to be widely accepted in the scientific community. The model was based on the plasma membrane's "railroad track" appearance in early electron micrographs. Davson and Danielli theorized that the plasma membrane's structure resembled a sandwich with the analogy of...
Membrane Fluidity01:26

Membrane Fluidity

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 a relatively...
Membrane Fluidity01:23

Membrane Fluidity

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.Fatty acids tails of phospholipids can be either saturated or...
Membrane Domains01:18

Membrane Domains

The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...

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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

t-SNARE protein conformations patterned by the lipid microenvironment.

Colin Rickman1, Claire N Medine, Alison R Dun

  • 1Centre for Integrative Physiology, School of Informatics, University of Edinburgh, Edinburgh EH8 9XD, Scotland, United Kingdom.

The Journal of Biological Chemistry
|January 23, 2010
PubMed
Summary

Target SNARE proteins (syntaxin and SNAP-25) form distinct conformations on the plasma membrane. Lipid order influences these protein structures, revealing how membrane environment shapes molecular interactions.

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Area of Science:

  • Cell biology
  • Biophysics
  • Membrane protein structure

Background:

  • The spatial distribution of target SNARE proteins (syntaxin and SNAP-25) is known.
  • However, their in situ conformations and interactions remain unclear.

Purpose of the Study:

  • To define the in situ conformations and interactions of syntaxin and SNAP-25.
  • To investigate the role of the lipid environment in shaping t-SNARE conformations.

Main Methods:

  • Super-resolution optical microscopy
  • Fluorescence lifetime imaging microscopy (FLIM)

Main Results:

  • Syntaxin and SNAP-25 form two distinct binary intermediate conformations within t-SNARE clusters.
  • These conformations are spatially segregated on the plasma membrane.
  • Disrupting lipid order caused all t-SNARE clusters to adopt a single, three-helical conformation.

Conclusions:

  • Spatially distinct t-SNARE intermediate states exist on the plasma membrane.
  • The lipid environment patterns t-SNARE conformation, influencing protein interactions.