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 Experiment Videos

SNARE complex regulation by phosphorylation.

Deborah A Snyder1, Marie L Kelly, Dixon J Woodbury

  • 1Department of Physiology and Developmental Biology, Brigham Young University, 574 WIDB, Provo, UT 84602, USA.

Cell Biochemistry and Biophysics
|May 9, 2006
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Multiple structural states in an intrinsically disordered protein, SNAP-25, using circular dichroism.

Biophysical journal·2025
Same author

A review of TNP-ATP in protein binding studies: benefits and pitfalls.

Biophysical reports·2022
Same author

Drunken lipid membranes, not drunken SNARE proteins, promote fusion in a model of neurotransmitter release.

Frontiers in molecular neuroscience·2022
Same author

Drunken Membranes: Short-Chain Alcohols Alter Fusion of Liposomes to Planar Lipid Bilayers.

Biophysical journal·2017
Same author

Functional ryanodine receptors in the membranes of neurohypophysial secretory granules.

The Journal of general physiology·2014
Same author

Is it zippered? Does it flare? That darn complexin clamping SNARE.

Biophysical journal·2013

Soluble N-ethylmaleimide-sensitive fusion factor attachment protein receptors (SNAREs) regulate neurotransmitter release. Enzymatic modifications, like phosphorylation, fine-tune SNARE complex activity and control the degree of vesicle exocytosis beyond calcium influx.

Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • SNAREs (soluble N-ethylmaleimide-sensitive fusion factor attachment protein receptors) are crucial for vesicular trafficking and neurotransmitter release in neurons.
  • While calcium influx triggers neurotransmitter release, it doesn't solely regulate the extent of exocytosis, indicating other regulatory factors are involved.

Purpose of the Study:

  • This review focuses on the role of enzymatic modifications, particularly phosphorylation, in regulating SNARE complex function.
  • Investigate how phosphorylation and other modifications like palmitoylation affect SNARE protein activity and neurotransmitter release.

Main Methods:

  • Review of existing literature on SNARE proteins and their enzymatic regulation.
  • Analysis of research identifying specific phosphorylation sites on SNAREs and interacting proteins.

Related Experiment Videos

  • Examination of the functional consequences of these post-translational modifications.

    • Main Results:

    • Phosphorylation of SNARE proteins and associated factors influences SNARE complex formation, stability, and disassembly.
    • Specific phosphorylation events have been identified that modulate the efficiency of neurotransmitter release.
    • Palmitoylation of SNAP-25 affects its localization and activity, further regulating exocytosis.

    Conclusions:

    • Enzymatic modifications, especially phosphorylation, are key regulators of SNARE complex function and neurotransmitter release.
    • Understanding these modifications provides insight into the precise control of exocytosis in neuronal signaling.
    • Further research into these regulatory mechanisms can elucidate pathways for neurological disorders.