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Related Concept Videos

ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

The P-type pumps are a large family of integral membrane transporter ATPases. They are divided into five major types based on substrate specificity, from I to V.
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...
Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

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...
Membrane Asymmetry Regulating Transporters01:19

Membrane Asymmetry Regulating Transporters

Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
ATP Synthase: Structure01:18

ATP Synthase: Structure

ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
Chemical Synapses01:26

Chemical Synapses

Chemical synapses are specialized sites between two neurons or between a neuron and a non-neuronal cell like a muscle, glandular or sensory cell.
Because chemical synapses depend on the release of neurotransmitter molecules from synaptic vesicles to pass on their signal, there is an approximately one millisecond delay between when the axon potential reaches the presynaptic terminal and when the neurotransmitter leads to opening of postsynaptic ion channels. Additionally, this signaling is...

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Related Experiment Video

Updated: Jun 10, 2026

Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient
08:06

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Published on: September 3, 2014

A plasma membrane Ca2+ ATPase isoform at the postsynaptic density.

A C Burette1, E E Strehler, R J Weinberg

  • 1Department of Cell and Developmental Biology, University of North Carolina at Chapel Hill, 314 Taylor Hall, CB# 7090, Chapel Hill, NC 27599, USA. alain_burette@med.unc.edu

Neuroscience
|August 4, 2010
PubMed
Summary

Researchers discovered that the PMCA2w protein is concentrated in the postsynaptic density (PSD) of hippocampal synapses. This finding suggests a new role for plasma membrane Ca(2+)-ATPase (PMCA) pumps in regulating calcium signaling within the synapse.

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Last Updated: Jun 10, 2026

Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient
08:06

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Published on: September 3, 2014

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Published on: April 2, 2014

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • Excitatory input in the hippocampus occurs at dendritic spines.
  • Calcium (Ca2+) entry via NMDA receptors triggers biochemical cascades affecting synaptic efficacy.
  • Dendritic spines limit Ca2+ diffusion to maintain signaling specificity.

Purpose of the Study:

  • To investigate the mechanisms of Ca2+ removal from dendritic spines.
  • To identify proteins involved in regulating Ca2+ homeostasis at the postsynaptic density (PSD).

Main Methods:

  • Light- and electron-microscopic immunohistochemistry were employed.
  • Localization of PMCA2w within hippocampal spines was examined.

Main Results:

  • PMCA2w, a plasma membrane Ca(2+)-ATPase (PMCA) isoform, was found to be concentrated at the PSD of most hippocampal spines.
  • This localization suggests PMCA2w is strategically positioned to influence subsynaptic Ca2+ levels.

Conclusions:

  • PMCA2w may form supramolecular complexes within the PSD.
  • This protein likely plays a role in regulating subsynaptic Ca2+ nanodomains.
  • PMCAs represent a novel class of modulators for synaptic Ca2+ signaling.