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Related Concept Videos

Plastic Deformations01:19

Plastic Deformations

470
Plastic deformation represents a fundamental concept in materials science, which explains the irreversible change in the shape of a material when it experiences stress beyond its elastic capability. This phenomenon is important in structural engineering, especially in designing and analyzing cantilever beams—structures that are securely fixed at one end and bear loads at the opposite end. When these beams are subjected to loads within their elastic range, they will return to their...
470
Plastic Deformations01:14

Plastic Deformations

455
It is essential to understand how structural members behave under plastic deformation when the bending stress exceeds the material's yield strength. This state of deformation permanently alters the shape of the member, in contrast to the linear elastic behavior observed before yielding. The strain at any point in the member is expressed in terms of maximum strain. Notably, the neutral axis, which coincides with the centroid during elastic bending, shifts away from the centroid under plastic...
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Antiepileptic Drugs: Modulators of Neurotransmitter Release Mediated by SV2A Protein01:20

Antiepileptic Drugs: Modulators of Neurotransmitter Release Mediated by SV2A Protein

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Antiepileptic drugs, such as levetiracetam (Keppra) and brivaracetam (Briviact), have emerged as crucial tools in managing epilepsy. These medications exert their therapeutic effects by targeting the synaptic vesicle protein SV2A, a transmembrane glycoprotein primarily found in the brain.
SV2A is a transmembrane glycoprotein located predominantly in the brain, modulating the release of neurotransmitters for neuronal communication. Both levetiracetam and brivaracetam exhibit a high affinity for...
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Temperature Dependent Deformation01:12

Temperature Dependent Deformation

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In a nonhomogeneous rod made up of steel and brass, restrained at both ends and subjected to a temperature change, several steps are involved in calculating the stress and compressive load. Due to the problem's static indeterminacy, one end support is disconnected, allowing the rod to experience the temperature change freely. Next, an unknown force is applied at the free end, triggering deformations in the rod's steel and brass portions. These deformations are then calculated and added...
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Deformations in a Symmetric Member in Bending01:18

Deformations in a Symmetric Member in Bending

521
When analyzing the deformation of a symmetric prismatic member subjected to bending by equal and opposite couples, it becomes clear that as the member bends, the originally straight lines on its wider faces curve into circular arcs, with a constant radius centered at a point known as Point C. This phenomenon helps to understand the stress and strain distribution within the member more clearly.
When the member is segmented into tiny cubic elements, it is observed that the primary stress...
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Related Experiment Video

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Imaging Plasma Membrane Deformations With pTIRFM
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Hsp90 Mediates Membrane Deformation and Exosome Release.

Elsa Lauwers1, Yu-Chun Wang1, Rodrigo Gallardo2

  • 1VIB-KU Leuven Center for Brain & Disease Research, 3000 Leuven, Belgium; KU Leuven, Department of Neurosciences, Leuven Brain Institute, 3000 Leuven, Belgium.

Molecular Cell
|September 8, 2018
PubMed
Summary

Heat shock protein 90 (Hsp90) directly deforms cell membranes using a conserved helix, promoting exosome release. This newly identified function is separate from its chaperone activity and is crucial for releasing exosomes.

Keywords:
Hsp90chaperoneexosomemembrane remodelingmultivesicular body

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Biochemistry

Background:

  • Heat shock protein 90 (Hsp90) is a crucial molecular chaperone, vital for maintaining proteome integrity and comprising approximately 2% of cellular protein.
  • Hsp90's canonical role involves assisting in the folding and stability of client proteins, but its potential involvement in membrane dynamics was unexplored.

Purpose of the Study:

  • To investigate the novel membrane-interacting and -deforming capabilities of Hsp90.
  • To elucidate the role of Hsp90 in exosome release, specifically its mechanism involving multivesicular bodies (MVBs).
  • To differentiate Hsp90's membrane-deforming function from its established chaperone activity.

Main Methods:

  • Utilized a novel cell-free system to study Hsp90-membrane interactions.
  • Performed in vivo measurements to assess Hsp90's function in live cells.
  • Analyzed the impact of Hsp90 conformational states (open vs. closed dimer) on membrane interaction and MVB fusion.

Main Results:

  • Identified an evolutionarily conserved amphipathic helix in Hsp90 responsible for direct membrane interaction and deformation.
  • Demonstrated that this amphipathic helix facilitates exosome release by promoting the fusion of MVBs with the plasma membrane.
  • Showed that stabilizing the open Hsp90 dimer conformation exposes the helix and promotes MVB fusion, while the closed state inhibits these effects.

Conclusions:

  • Hsp90 possesses a previously unrecognized function in deforming membranes via an amphipathic helix.
  • This membrane-deforming activity is structurally distinct from Hsp90's chaperone function.
  • Hsp90's ability to deform membranes is essential for the release of exosomes through MVB fusion.