Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Pinching-off of Coated Vesicles

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...

Fusion of Secretory Vesicles with the Plasma Membrane

Fusion of Secretory Vesicles with the Plasma Membrane

Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...

Overview of Secretory Vesicles

Overview of Secretory Vesicles

Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...

COP Coated Vesicles

COP Coated Vesicles

Membrane-enclosed structures called vesicles transport proteins and lipids across the cell. The vesicles derive their cargo from the plasma membrane, Golgi, ER, or endosome. Coated vesicles are spherical, protein-coated carriers with a 50–100 nm diameter that mediate bidirectional transport between the ER and the Golgi. The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. Their formation is driven by the assembly of...

Regulation of Nuclear Protein Sorting

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...

Protein Complex Assembly

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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

The chaperone DNAJB6b halts amyloid formation through association with transient Aβ oligomers.

Physical chemistry chemical physics : PCCP·2026

Same author

Growth of fatty acid vesicles coupled with amino acid sequences of peptides toward evolvable protocells.

Communications chemistry·2026

Same author

The temperature dependence of amyloid <i>β</i> solubility reveals the hydrophobic effect as the main driving force for fibril formation.

Proceedings of the National Academy of Sciences of the United States of America·2026

Same author

Rapid elongation drives the exceptionally fast aggregation of the most common localized human amyloid medin.

Communications chemistry·2026

Same author

Transient Interactions of α-Synuclein N- and C-Termini.

ACS chemical neuroscience·2026

Same author

Supramolecular Assembly of Collagen-Mimetic Peptide D-Periodic Fibrils and Nanoassemblies.

Biomacromolecules·2026

Same journal

Nanopore sequencing with proteins: synchronization and dischronization of molecular dynamics simulations with laboratory and industrial developments.

Soft matter·2026

Same journal

Catanionics from biosurfactants and regular surfactants: miscibility and structure.

Soft matter·2026

Same journal

Adhesives with a thickness smaller than the fractocohesive length enhance adhesion.

Soft matter·2026

Same journal

Non-equilibrium phase transitions in hybrid Voronoi models of cell colonies.

Soft matter·2026

Same journal

Effects of methoxy substituents on self-assembly and gelation performance of benzamide-based organogelators.

Soft matter·2026

Same journal

Rheology of <i>Escherichia coli</i> suspensions with various bacterial morphologies and motion characteristics.

Soft matter·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Jun 2, 2025

Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

Published on: June 26, 2018

α-Synuclein interaction with POPC/POPS vesicles.

Marija Dubackic¹, Veronica Lattanzi^1,2, Yun Liu^3,4

¹Physical Chemistry, Chemistry Centre, Lund University, SE-22100 Lund, Sweden. majuskad@hotmail.com.

|January 13, 2025

Summary

This summary is machine-generated.

Alpha-synuclein (αSyn) protein binds to anionic lipid vesicles, forming alpha-helical structures. Fibril formation triggers vesicle fusion, doubling vesicle size.

More Related Videos

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Published on: August 13, 2017

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Published on: September 28, 2019

Related Experiment Videos

Last Updated: Jun 2, 2025

Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

Published on: June 26, 2018

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Published on: August 13, 2017

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Published on: September 28, 2019

Area of Science:

Biochemistry
Biophysics
Neuroscience

Background:

Alpha-synuclein (αSyn) is an amyloid-forming protein implicated in neurodegenerative diseases.
Small unilamellar vesicles (SUVs) are model systems for cell membranes.

Purpose of the Study:

To investigate the adsorption of αSyn monomers onto SUVs composed of zwitterionic (POPC) and anionic (POPS) lipids.
To understand the structural changes and vesicle dynamics during αSyn fibril formation.

Main Methods:

Studied αSyn adsorption onto mixed lipid vesicles (POPC/POPS).
Analyzed secondary structure changes of adsorbed αSyn.
Investigated vesicle size changes during seeded fibril formation.

Main Results:

αSyn monomers adsorb to anionic POPS-containing vesicles, adopting an α-helical structure.
Adsorption is dependent on the POPS fraction, considering electrostatic shifts.
Seeded fibril formation induced vesicle fusion, approximately doubling average vesicle size.

Conclusions:

αSyn adsorption onto anionic lipid membranes is concentration and lipid composition-dependent.
Vesicle fusion is a key event during αSyn fibril formation on membranes.