Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
Membrane bending can happen due to intrinsic changes in lipid composition or extrinsic association with different proteins. The proteins involved...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

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 cytoskeletal...
SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Polarity of the Cytoskeleton01:18

Polarity of the Cytoskeleton

The intrinsic polarity of cells can be primarily attributed to two factors- i) the asymmetric accumulation of mobile components such are regulatory molecules and subcellular components across the cell and ii) the orientation of polar cytoskeletal filaments that make up the cytoskeletal networks, specifically microfilaments, and microtubules arranged along the axis of polarity. Interactions between the cytoskeletal filaments are crucial for the establishment and maintenance of the polar nature...

You might also read

Related Articles

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

Sort by
Same author

Lipofuscin accumulation in aging and CLN1 is associated with deficient de-S-acylation, lyso-mitochondrial dysfunction, and lipid dyshomeostasis.

Acta neuropathologica·2026
Same author

Deficient de-S-acylation in aging and CLN1 contributes to lyso-mitochondrial dysfunction, lipid dyshomeostasis, and resultant lipofuscin biogenesis.

Research square·2026
Same author

UV induces common cutaneous amyloid-like melanosomal protein aggregates.

bioRxiv : the preprint server for biology·2025
Same author

Synaptic vesicle endocytosis deficits underlie cognitive dysfunction in mouse models of GBA-linked Parkinson's disease and dementia with Lewy bodies.

Nature communications·2025
Same author

Molecular elucidation of brain lipofuscin in aging and Neuronal Ceroid Lipofuscinosis.

Research square·2025
Same author

Synaptic vesicle endocytosis deficits underlie GBA-linked cognitive dysfunction in Parkinson's disease and Dementia with Lewy bodies.

Research square·2025

Related Experiment Video

Updated: May 16, 2026

Pulling Membrane Nanotubes from Giant Unilamellar Vesicles
06:26

Pulling Membrane Nanotubes from Giant Unilamellar Vesicles

Published on: December 7, 2017

Monomeric synucleins generate membrane curvature.

Christopher H Westphal1, Sreeganga S Chandra

  • 1Program in Cellular Neuroscience, Neurodegeneration and Repair, Yale University, New Haven, Connecticut 06536, USA.

The Journal of Biological Chemistry
|November 28, 2012
PubMed
Summary

Synucleins, including alpha-synuclein linked to Parkinson disease, can generate membrane curvature. This function is dependent on protein structure, suggesting a new role for synucleins in membrane dynamics.

More Related Videos

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time
07:56

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time

Published on: May 30, 2021

Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions
06:32

Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions

Published on: July 28, 2022

Related Experiment Videos

Last Updated: May 16, 2026

Pulling Membrane Nanotubes from Giant Unilamellar Vesicles
06:26

Pulling Membrane Nanotubes from Giant Unilamellar Vesicles

Published on: December 7, 2017

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time
07:56

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time

Published on: May 30, 2021

Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions
06:32

Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions

Published on: July 28, 2022

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Protein Biochemistry

Background:

  • Synucleins are presynaptic proteins, with alpha-synuclein mutations causing familial Parkinson disease.
  • Understanding synuclein's molecular function is crucial for Parkinson disease research.
  • Previous studies highlighted synucleins' role in synaptic function.

Purpose of the Study:

  • To investigate the molecular functions of synucleins.
  • To identify synaptic protein changes in synuclein knock-out brains.
  • To explore the relationship between synucleins and membrane curvature dynamics.

Main Methods:

  • Unbiased proteomic screening of alpha, beta, and gamma synuclein knock-out brains.
  • Quantification of synaptic protein levels, focusing on membrane curvature proteins.
  • In vitro assays to assess synuclein's ability to generate membrane curvature.
  • Analysis of different alpha-synuclein forms (monomeric, tetrameric, mutant A30P).

Main Results:

  • Synuclein knock-out brains show altered levels of membrane curvature proteins, notably endophilin A1.
  • Synucleins, like endophilins, can generate membrane curvature.
  • Monomeric alpha-synuclein, but not tetrameric or A30P mutant, effectively bends membranes.
  • Synuclein's membrane bending activity relies on its N-terminal amphipathic helix.

Conclusions:

  • Synucleins and endophilin A1 levels are reciprocally regulated and functionally linked.
  • Synucleins are proposed as a class of proteins that sense and generate membrane curvature.
  • These findings offer new insights into the physiological roles of synucleins in neuronal function.