Related Experiment Video
Updated: Apr 3, 2026

06:45
In Vivo Single-Molecule Tracking at the Drosophila Presynaptic Motor Nerve Terminal
Published on: January 14, 2018
9.0K
Differential Effects of Munc18s on Multiple Degranulation-Relevant Trans-SNARE Complexes
Hao Xu1, Matthew Grant Arnold1, Sushmitha Vijay Kumar1
1Department of Biological Sciences, University of Southern Mississippi, Hattiesburg, Mississippi, United States of America.
Plos One
|September 19, 2015
Summary
Mast cell exocytosis involves SNARE proteins. This study identifies six trans-SNARE complexes and reveals Munc18a
Area of Science:
- Cell Biology
- Molecular Biology
- Immunology
Background:
- Mast cell exocytosis is crucial for immune responses.
- This process relies on SNARE proteins for vesicle fusion.
- The specific pairing and regulation of SNAREs remain unclear.
Purpose of the Study:
- To comprehensively examine SNARE complex formation in mast cell exocytosis.
- To identify functional trans-SNARE complexes involving Q-SNAREs and R-SNAREs.
- To elucidate the regulatory role of Munc18 proteins in SNARE-mediated fusion.
Main Methods:
- In vitro assays to test SNARE complex formation.
- Lipid mixing assays to assess fusion.
- Investigating the effects of Munc18 proteins on SNARE complex activity.
Main Results:
- Identified six distinct trans-SNARE complexes (e.g., VAMP2/syntaxin3/SNAP-23).
- Munc18a synergistically enhanced fusion with SNAP-23-based SNARE complexes.
- Munc18a protected SNAREs from inhibitory domains, suggesting a regulatory role.
Conclusions:
- Established specific SNARE pairings critical for mast cell exocytosis.
- Confirmed Munc18a's essential role in mast cell fusion, acting synergistically with SNAREs.
- Post-translational modifications may regulate Munc18b/c activity in mast cell degranulation.
Related Concept Videos
SNAREs and Membrane Fusion
13.6K
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...
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...
13.6K
Fusion of Secretory Vesicles with the Plasma Membrane
19.5K
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...
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
19.5K
Receptor Downregulation in MVBs
3.0K
Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that lead to cell proliferation, migration, and differentiation. Overexpression of EGFR stimulates cells to proliferate. Excessive EGFR...
The EGFR can initiate signaling pathways that lead to cell proliferation, migration, and differentiation. Overexpression of EGFR stimulates cells to proliferate. Excessive EGFR...
3.0K
Assembly of Signaling Complexes
7.2K
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,...
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
7.2K
Pinching-off of Coated Vesicles
4.4K
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...
4.4K
Overview of Secretory Vesicles
9.9K
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...
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
9.9K

