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Related Concept Videos

Internal Receptors01:31

Internal Receptors

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Many cellular signals are hydrophilic and therefore cannot pass through the plasma membrane. However, small or hydrophobic signaling molecules can cross the hydrophobic core of the plasma membrane and bind to internal, or intracellular, receptors that reside within the cell. Many mammalian steroid hormones use this mechanism of cell signaling, as does nitric oxide (NO) gas.
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Internal Energy02:00

Internal Energy

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The total of all possible kinds of energy present in a substance is called the internal energy (U), sometimes symbolized as E. Suppose a system with initial internal energy, Uinitial, undergoes a change in energy (transfer of work or heat), and the final internal energy of the system is Ufinal. Change in internal energy equals the difference between Ufinal and Uinitial.
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Internal Energy01:29

Internal Energy

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The internal energy of a thermodynamic system is the sum of the kinetic and potential energies of all the molecules or entities in the system. The kinetic energy of an individual molecule includes contributions due to its rotation and vibration, as well as its translational energy. The potential energy is associated only with the interactions between one molecule and the other molecules of the system. Neither the system's location nor its motion is of any consequence as far as the internal...
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The Equilibrium Binding Constant and Binding Strength02:18

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The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
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Introduction to Membrane Proteins01:16

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The cell membrane, or plasma membrane, is an ever-changing landscape. It is described as a fluid mosaic where various macromolecules are embedded in the phospholipid bilayer. Among the macromolecules are proteins. The protein content varies across cell types. For example, mitochondrial inner membranes contain ~76% protein content, while myelin contains ~18% protein content. Individual cells contain many types of membrane proteins—red blood cells contain over 50—and different cell...
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Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Related Experiment Video

Updated: Feb 6, 2026

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

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Membrane binding, internalization, and sorting of alpha-synuclein in the cell.

Caterina Masaracchia1, Marilena Hnida1, Ellen Gerhardt1

  • 1Department of Experimental Neurodegeneration, Center for Biostructural Imaging of Neurodegeneration, Center for Nanoscale Microscopy and Molecular Physiology of the Brain, University Medical Center Goettingen, 37073, Göttingen, Germany.

Acta Neuropathologica Communications
|August 16, 2018
PubMed
Summary

Alpha-synuclein internalization into cells involves membrane binding and the endocytic pathway. Rab proteins are key to processing and clearing alpha-synuclein, offering potential therapeutic targets for Parkinson's disease.

Keywords:
Alpha-synucleinParkinson’s diseaseRab proteinsSpreadingUptake

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Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains
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Related Experiment Videos

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Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains
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Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • Alpha-synuclein (aSyn) misfolding and aggregation are hallmarks of Parkinson's disease (PD) and other synucleinopathies.
  • The exact molecular mechanisms linking aSyn to disease pathology and its cellular uptake remain unclear.
  • aSyn can spread between neurons, contributing to disease progression.

Purpose of the Study:

  • To investigate the interaction of alpha-synuclein with cellular membranes and trafficking pathways.
  • To elucidate the mechanisms of aSyn internalization and intracellular processing.
  • To identify potential therapeutic targets for synucleinopathies.

Main Methods:

  • Utilized cellular models of Parkinson's disease.
  • Investigated aSyn internalization using dynamin inhibitors.
  • Screened Rab-GTPase proteins for their role in aSyn trafficking.
  • Analyzed aSyn colocalization with endocytic and autophagy-lysosomal markers.

Main Results:

  • Membrane binding is crucial for aSyn internalization.
  • aSyn uptake is dependent on the endocytic pathway, specifically involving membrane scission.
  • Internalized aSyn colocalizes with Rab5A, Rab7, and Rab4A, indicating involvement in endosomal trafficking.
  • aSyn is eventually routed to the autophagy-lysosomal pathway for degradation.
  • Rab proteins play a significant role in modulating aSyn processing, clearance, and spread.

Conclusions:

  • Cellular internalization of alpha-synuclein is an active process mediated by membrane interactions and endocytosis.
  • Rab proteins are critical regulators of alpha-synuclein intracellular fate and neuronal spread.
  • Targeting Rab proteins presents a promising therapeutic strategy for Parkinson's disease and related disorders.