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Related Concept Videos

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.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
Assembly of the Lipid Bilayer in the ER01:28

Assembly of the Lipid Bilayer in the ER

Biological membranes are more than just a barrier separating cell cytoplasm from the outside environment. They are highly dynamic and help maintain the integrity and physiological stability of the cells as well as membrane-bound organelles. Membranes also play vital roles in cell-to-cell and intracellular communication.
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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
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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...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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Protein Complex Assembly

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Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis
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Published on: July 16, 2020

Membrane lipids influence protein complex assembly-disassembly.

Leah Shin1, Won Jin Cho, Jeremy D Cook

  • 1Department of Physiology, Wayne State University School of Medicine, Detroit, Michigan 48201, USA.

Journal of the American Chemical Society
|April 9, 2010
PubMed
Summary
This summary is machine-generated.

Cholesterol-associated vesicles yield smaller t-/v-SNARE ring complexes compared to L-alpha-lysophosphatidylcholine (LPC) vesicles. LPC also promotes N-ethylmaleimide-sensitive factor + adenosine triphosphate-induced disassembly of beta-sheet structures in these complexes.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Soluble NSF Attachment Protein Receptors (SNAREs) mediate membrane fusion, a critical process in cellular transport.
  • The precise structural mechanisms and lipid interactions governing SNARE complex assembly and disassembly remain incompletely understood.
  • Understanding SNARE complex dynamics is crucial for deciphering intracellular trafficking pathways.

Purpose of the Study:

  • To investigate the influence of different lipids, specifically cholesterol and L-alpha-lysophosphatidylcholine (LPC), on the structural properties of t-/v-SNARE complexes.
  • To elucidate the role of N-ethylmaleimide-sensitive factor (NSF) and adenosine triphosphate (ATP) in modulating SNARE complex structure in the presence of distinct lipid environments.

Main Methods:

  • Atomic Force Microscopy (AFM) was employed to measure the size of t-/v-SNARE ring complexes formed with cholesterol-associated vesicles versus LPC-containing vesicles.
  • Circular Dichroism (CD) spectroscopy was utilized to analyze the secondary structural changes (beta-sheet and alpha-helical content) within t-/v-SNARE complexes under different conditions.

Main Results:

  • t-/v-SNARE ring complexes formed with cholesterol-associated vesicles were approximately 11% smaller than those formed with LPC-containing vesicles.
  • CD spectroscopy revealed that in the presence of LPC, NSF + ATP induced a significant disassembly of beta-sheet structures within the t-/v-SNARE complex.
  • The alpha-helical content of the t-/v-SNARE complex remained largely unaffected by NSF + ATP in the presence of LPC.

Conclusions:

  • Cholesterol and LPC differentially regulate the size and structural integrity of t-/v-SNARE complexes.
  • LPC, in conjunction with NSF and ATP, facilitates the disruption of beta-sheet secondary structures in SNARE complexes, suggesting a lipid-mediated mechanism for SNARE disassembly.
  • These findings highlight the importance of the lipid microenvironment in controlling SNARE complex function and membrane fusion regulation.