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Related Concept Videos

Ion Channels01:19

Ion Channels

The movement of ions like sodium, potassium, and calcium into and out of the cell is essential to maintain the electrochemical gradient in living cells. The ion channels—a class of membrane transport proteins—help maintain this ionic gradient for the smooth functioning of physiological activities such as maintaining cell size and volume, conducting nerve impulses, and gas and nutrient exchange.
Ion channels are specialized integral membrane proteins on the plasma membrane that allow specific...
Electrical Synapses01:28

Electrical Synapses

Electrical synapses found in all nervous systems play important and unique roles. In these synapses, the presynaptic and postsynaptic membranes are very close together (3.5 nm) and are actually physically connected by channel proteins forming gap junctions.
Gap junctions allow the current to pass directly from one cell to the next. In contrast, in the chemical synapse, the neurotransmitters carry the information through the synaptic cleft from one neuron to the next. They consist of two...
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...
The Role of Ion Channels in Neuronal Computation01:19

The Role of Ion Channels in Neuronal Computation

A postsynaptic neuron usually receives numerous impulses from several other presynaptic neurons. The axon hillock of the postsynaptic neuron integrates all these signals and determines the likelihood of firing an action potential.
Sometimes a single EPSP is strong enough to induce an action potential in the postsynaptic neuron. However, multiple presynaptic inputs must often create EPSPs around the same time for the postsynaptic neuron to be sufficiently depolarized to fire an action potential.
Facilitated Transport01:19

Facilitated Transport

The chemical and physical properties of plasma membranes cause them to be selectively permeable. Since plasma membranes have both hydrophobic and hydrophilic regions, substances need to be able to transverse both regions. The hydrophobic area of membranes repels substances such as charged ions. Therefore, such substances need special membrane proteins to cross a membrane successfully. In  facilitated transport, also known as facilitated diffusion, molecules and ions travel across a membrane via...

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Updated: Jul 10, 2026

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo
09:44

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

Published on: June 2, 2019

Helical alpha-synuclein forms highly conductive ion channels.

Stanislav D Zakharov1, John D Hulleman, Elena A Dutseva

  • 1Departments of Biological Sciences, Purdue University, West Lafayette, Indiana 47907-2054, USA.

Biochemistry
|November 23, 2007
PubMed
Summary
This summary is machine-generated.

Monomeric alpha-synuclein forms ion channels in membranes, potentially impacting Parkinson's disease (PD) pathology. Familial PD mutants E46K and A53T formed channels, while A30P did not, suggesting distinct roles in PD.

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Cell Biology

Background:

  • Alpha-synuclein (alphaS) is implicated in Parkinson's disease (PD) pathogenesis.
  • AlphaS adopts a helical structure upon binding to negatively charged membranes, exhibiting membrane-permeabilizing activity.
  • Oligomeric forms of alphaS have been primarily associated with membrane permeabilization.

Purpose of the Study:

  • To investigate the mechanism of alpha-synuclein's membrane interaction and channel formation.
  • To compare the channel-forming capabilities of wild-type alphaS and familial PD mutants (E46K, A53T, A30P).
  • To elucidate the role of membrane properties and calcium ions in alphaS-mediated channel activity.

Main Methods:

  • Formation of ion channels by monomeric alphaS and mutants in lipid bilayers with specific compositions (anionic lipid, phosphatidylethanolamine).
  • Electrophysiological recordings to determine channel conductance states.
  • Far-UV circular dichroism (CD) to assess alpha-helical content and thermal stability.
  • Fluorescence correlation spectroscopy (FCS) to measure lateral mobility of membrane-bound alphaS.

Main Results:

  • Monomeric wild-type alphaS, E46K, and A53T mutants formed ion channels with defined conductance in anionic lipid/PE membranes under a trans-negative potential.
  • The familial PD mutant A30P, with lower membrane affinity, did not form channels.
  • Calcium ions inhibited channel formation and reduced conductance.
  • Oligomeric alphaS permeabilized membranes without forming discrete channels, independent of PE lipid or membrane potential.
  • Channel activity correlated with alpha-helical content, thermal stability, and lateral mobility of membrane-bound alphaS.

Conclusions:

  • Monomeric alphaS, in an alpha-helical conformation, forms discrete ion channels in membranes under a membrane potential.
  • These alphaS-formed ion channels may play a role in both the normal function and the pathophysiology of Parkinson's disease.
  • Different familial PD mutations exhibit distinct membrane interaction properties, influencing channel formation.