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Related Concept Videos

Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

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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.
Another mechanism for membrane domain formation involves membrane proteins interacting with...
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Microtubule Instability02:17

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Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated...
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Fluid Mosaic Model01:19

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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...
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Membrane Fluidity01:26

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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
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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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Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...
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Stabilization and structural analysis of a membrane-associated hIAPP aggregation intermediate.

Diana C Rodriguez Camargo1,2,3, Kyle J Korshavn2, Alexander Jussupow1

  • 1Institute for Advanced Study, Technische Universität München, Garching, Germany.

Elife
|November 18, 2017
PubMed
Summary

Researchers determined the structure of a key intermediate in amyloid formation using nanodiscs. This finding offers insights into type-2 diabetes pathology and protein misfolding diseases.

Keywords:
Amyloid peptideNMRStructurebiochemistrybiophysicsmembranenonestructural biology

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Neurodegenerative Diseases

Background:

  • Amyloid formation is linked to human diseases, with aggregating species causing cell death.
  • Understanding membrane-associated amyloid intermediates is crucial for disease pathology insights and therapeutic development.
  • Previous studies faced challenges in characterizing these intermediates due to cell membrane interactions.

Purpose of the Study:

  • To determine the structure of a human islet amyloid polypeptide (HIAPP) intermediate implicated in type-2 diabetes.
  • To investigate the role of membrane interactions in amyloid formation and propagation.
  • To establish a method for stabilizing and studying amyloid intermediates.

Main Methods:

  • Utilized Nuclear Magnetic Resonance (NMR) experimental constraints.
  • Employed nanodisc technology to stabilize the amyloid intermediate.
  • Performed ROSETTA and Molecular Dynamics (MD) simulations for structural analysis.

Main Results:

  • Solved the structure of a type-2 diabetes-related HIAPP intermediate.
  • Identified a unique β-strand structure, differing from typical amyloid β-hairpins.
  • Revealed flexibility and accessibility of the nucleating NFGAIL region within the intermediate.

Conclusions:

  • The study provides a novel structure of a membrane-associated amyloid intermediate.
  • The findings suggest a mechanism for the propagation of membrane-associated amyloid aggregation.
  • Nanodisc technology is a powerful tool for dissecting complex protein misfolding pathways.