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Related Concept Videos

Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

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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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SNAREs and Membrane Fusion01:43

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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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Overview of Secretory Vesicles01:33

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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.
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Gap Junctions01:27

Gap Junctions

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The cytoplasm of adjacent animal cells can exchange small molecules, ions, and secondary messengers via the communication channels which form the gap junctions. These junctions comprise a few hundred to thousands of molecular channels, each made of two halves, called the connexon hemichannel. A connexon is a hexamer of six transmembrane connexin proteins, which assemble radially, thus forming a pore or channel in the center. One connexon hemichannel docks with a corresponding connexon on the...
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Mechanisms of Membrane Domain Formation00:59

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Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
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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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Related Experiment Video

Updated: Sep 2, 2025

Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient
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Complexin Membrane Interactions: Implications for Synapse Evolution and Function.

Justine A Lottermoser1, Jeremy S Dittman1

  • 1Department of Biochemistry, Weill Cornell Medicine, New York, NY, United States.

Journal of Molecular Biology
|August 5, 2022
PubMed
Summary
This summary is machine-generated.

Complexin, a key protein in chemical synaptic transmission, has unclear functions. This review explores its membrane interactions, shedding light on its role in synaptic vesicle fusion and evolution.

Keywords:
amphipathic helixcomplexincurvaturemembranesynapse

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Last Updated: Sep 2, 2025

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Chemical synaptic transmission relies on proteins like complexin, crucial for synaptic vesicle fusion.
  • While SNARE-binding properties of complexin are understood, its membrane interactions remain less explored.
  • Complexin's diverse roles across species and synapses highlight a need for mechanistic clarity.

Purpose of the Study:

  • To review the known membrane interactions of the complexin C-terminal domain.
  • To explore the functional significance of complexin's membrane binding.
  • To discuss the relevance of membrane interactions to complexin's synaptic localization and evolutionary history.

Main Methods:

  • Literature review of studies on complexin's biochemical, structural, and functional properties.
  • Analysis of research focusing on complexin's C-terminal domain and membrane interactions.
  • Synthesis of findings regarding complexin's role in synaptic vesicle fusion.

Main Results:

  • Complexin exhibits conserved SNARE-binding properties.
  • Membrane-binding features of complexin are less understood but potentially significant.
  • Complexin's C-terminal domain interactions with membranes are key to its function.

Conclusions:

  • Understanding complexin's membrane interactions is crucial for elucidating its fundamental mechanisms in synaptic transmission.
  • Further research into complexin's membrane binding will clarify its synaptic localization and evolutionary path.
  • Complexin's multifaceted roles are likely influenced by its interactions with both SNAREs and membranes.