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Related Concept Videos

Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
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...
Fusion of Secretory Vesicles with the Plasma Membrane01:26

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...
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
The Spindle Assembly Checkpoint02:19

The Spindle Assembly Checkpoint

The spindle assembly checkpoint is a molecular surveillance mechanism ensuring the fidelity of chromosome segregation during anaphase. The checkpoint monitors the completion of all the prerequisite steps before chromosome segregation to determine whether the segregation process should proceed or be delayed.
Many proteins function together to control the spindle assembly checkpoint. Mutations affecting these proteins may allow cells to proceed into anaphase prematurely, resulting in the...
Protein Complex Assembly02:41

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...

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Related Experiment Video

Updated: Jun 6, 2026

Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient
08:06

Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient

Published on: September 3, 2014

CSPα promotes SNARE-complex assembly by chaperoning SNAP-25 during synaptic activity.

Manu Sharma1, Jacqueline Burré, Thomas C Südhof

  • 1Department of Molecular and Cellular Physiology, Stanford University, SIM1, 265 Campus Drive, Palo Alto, CA 94304-5453, USA. sharma11@stanford.edu

Nature Cell Biology
|December 15, 2010
PubMed
Summary

The protein CSPα prevents neurodegeneration by chaperoning SNAP-25, a key component of synaptic vesicle fusion. Its absence leads to SNAP-25 aggregation and degradation, causing severe neuronal damage.

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Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay

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Related Experiment Videos

Last Updated: Jun 6, 2026

Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient
08:06

Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient

Published on: September 3, 2014

Presynapse Formation Assay Using Presynapse Organizer Beads and “Neuron Ball” Culture
10:17

Presynapse Formation Assay Using Presynapse Organizer Beads and “Neuron Ball” Culture

Published on: August 2, 2019

Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay
09:19

Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay

Published on: October 19, 2012

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • Neurons form numerous presynaptic terminals crucial for neurotransmission.
  • The protein CSPα is localized to presynaptic terminals and forms a complex with Hsc70 and SGT.
  • CSPα deletion causes severe neurodegeneration in mice and flies.

Purpose of the Study:

  • To investigate the role of CSPα in maintaining presynaptic function and preventing neurodegeneration.
  • To elucidate the mechanism by which CSPα influences SNARE complex formation and SNAP-25 stability.

Main Methods:

  • Analysis of CSPα-knockout mice and flies.
  • Biochemical assays to study protein-protein interactions and complex formation.
  • Investigation of SNAP-25 aggregation, ubiquitylation, and degradation pathways.

Main Results:

  • The CSPα-Hsc70-SGT complex directly binds monomeric SNAP-25, preventing its aggregation.
  • CSPα deletion leads to an abnormal SNAP-25 conformer that inhibits SNARE complex formation and promotes its degradation.
  • Synaptic activity regulates SNAP-25 degradation, a process modulated by CSPα levels.

Conclusions:

  • CSPα acts as a crucial chaperone for SNAP-25, maintaining SNARE complex formation and synaptic vesicle fusion.
  • A balance between CSPα-dependent chaperoning and ubiquitin-dependent degradation regulates SNAP-25 function in presynaptic terminals.
  • This study reveals a unique protein quality-control mechanism essential for neuronal survival.