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Related Concept Videos

SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

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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...
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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...
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Protein Complexes with Interchangeable Parts01:57

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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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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
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Pinching-off of Coated Vesicles01:32

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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...
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Protein Complex Assembly

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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.
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Related Experiment Video

Updated: Jun 15, 2025

Detergent-free Ultrafast Reconstitution of Membrane Proteins into Lipid Bilayers Using Fusogenic Complementary-charged Proteoliposomes.
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SuFEx Chemistry Enables Covalent Assembly of a 280-kDa 18-Subunit Pore-Forming Complex.

Lee Schnaider1,2, Sophia Tan1,2, Pratik R Singh3

  • 1Department of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, California 94143, United States.

Journal of the American Chemical Society
|August 27, 2024
PubMed
Summary

Researchers used SuFEx chemistry to covalently stabilize large protein assemblies, like the CsgG:CsgF pore complex. This method enhances structural stability and homogeneity for applications such as DNA sequencing.

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Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
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Last Updated: Jun 15, 2025

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SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy
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Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
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Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Chemical Biology

Background:

  • Proximity-enhanced chemical cross-linking is vital for studying protein interactions and drug development.
  • Large macromolecular assemblies require robust stabilization for advanced applications like DNA sequencing.

Purpose of the Study:

  • To covalently stabilize the large, 18-subunit CsgG:CsgF pore complex using SuFEx chemistry.
  • To enhance the structural integrity and homogeneity of the CsgG:CsgF complex for improved performance in applications such as DNA sequencing.

Main Methods:

  • Design and synthesis of CsgF derivatives functionalized with sulfonyl fluorides.
  • Application of SuFEx click chemistry for covalent stabilization of the CsgG:CsgF complex.
  • Characterization of the stabilized complex and its channel-forming properties in artificial membranes.
  • Molecular dynamics simulations to investigate reaction mechanisms.

Main Results:

  • A highly stable, covalently cross-linked CsgG:CsgF complex was formed with very high yield.
  • The SuFEx reaction demonstrated a rapid rate and high efficiency.
  • The resulting pores exhibited high homogeneity when reconstituted into artificial membranes.
  • Molecular dynamics simulations revealed the reaction mechanism involving SO2F groups and targeted tyrosine residues.

Conclusions:

  • SuFEx chemistry is effective for the structural stabilization of large macromolecular assemblies (up to 280 kDa).
  • The covalent stabilization significantly enhances the robustness and homogeneity of the CsgG:CsgF pore complex.
  • This approach holds promise for improving the stability of protein-based nanomaterials for biotechnological applications.