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

SNAP-29 is a promiscuous syntaxin-binding SNARE.

A C Hohenstein1, P A Roche

  • 1Experimental Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, MD 2089, USA.

Biochemical and Biophysical Research Communications
|July 11, 2001
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

Disruption of protein complexes containing protein phosphatase 2B and Munc18c reduces the secretion of von Willebrand factor from endothelial cells.

Journal of thrombosis and haemostasis : JTH·2017
Same author

The last exon of SNAP-23 regulates granule exocytosis from mast cells.

The Journal of biological chemistry·2001
Same author

Protecting genetic privacy.

Nature reviews. Genetics·2001
Same author

Concentration of MHC class II molecules in lipid rafts facilitates antigen presentation.

Nature immunology·2001
Same author

Intracellular redirection of plasma membrane trafficking after loss of epithelial cell polarity.

Molecular biology of the cell·2000
Same author

Identification of syntaxin 1A as a novel binding protein for presenilin-1.

Brain research. Molecular brain research·2000
Same journal

NAT10-mediated RNA N4-acetylation promotes intestinal fibroblast senescence via DHRS2.

Biochemical and biophysical research communications·2026
Same journal

Deciphering potent MPL activation by the fucose-binding lectin thrombocorticin.

Biochemical and biophysical research communications·2026
Same journal

Mitochondrial genome alterations in cancer: From mutations and epigenetics to targeted therapiesack.

Biochemical and biophysical research communications·2026
Same journal

GPC3 chimeric antigen receptor (CAR)-NK cells combined with Enoblituzumab enhance the anti-tumor efficacy against hepatocellular carcinoma.

Biochemical and biophysical research communications·2026
Same journal

A miR-382-5p-PORCN axis modulates endogenous Wnt signaling during palatal development.

Biochemical and biophysical research communications·2026
Same journal

Development of a vitamin-related gene signature to predict the immune characteristics and prognosis of glioma.

Biochemical and biophysical research communications·2026
See all related articles

Soluble NSF Attachment Protein Receptors (SNAREs) mediate membrane fusion. SNAP-23 and SNAP-29 SNARE proteins show distinct binding preferences, suggesting specialized roles in cellular transport.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Soluble NSF Attachment Protein Receptors (SNAREs) are crucial for membrane fusion specificity.
  • Organelle-specific syntaxins form heterodimers with SNAP-23 or its homolog SNAP-29.
  • Understanding the differential binding of SNAP-23 and SNAP-29 is key to elucidating intracellular trafficking pathways.

Purpose of the Study:

  • To investigate the differential binding affinities of SNAP-23 and SNAP-29 for various syntaxins.
  • To determine the functional implications of these differential interactions in membrane fusion events.

Main Methods:

  • In vitro and in vivo binding assays were employed.
  • Analysis of binary SNARE complex formation between syntaxins, SNAP-23, and SNAP-29.

Related Experiment Videos

  • Assessment of how vesicle-associated SNAREs influence SNAP-29 binding.

    • Main Results:

    • SNAP-23 preferentially binds to plasma membrane syntaxins.
    • SNAP-29 exhibits equal binding affinity for both plasma membrane and intracellular syntaxins.
    • SNAP-29 binding is augmented by syntaxin's interaction with vesicle-associated SNAREs, and vice versa.

    Conclusions:

    • SNAP-23 is likely involved in regulating plasma membrane-vesicle fusion.
    • SNAP-29 plays a significant role in maintaining diverse intracellular protein trafficking pathways.
    • Differential SNARE complex formation underlies the specificity of cellular membrane fusion events.