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Related Concept Videos

Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

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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.
Another mechanism for membrane domain formation involves membrane proteins interacting with...
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Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

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Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
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Membrane Domains01:18

Membrane Domains

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The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the...
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IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

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Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and...
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Long-term Potentiation01:35

Long-term Potentiation

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Long-term potentiation, or LTP, is one of the ways by which synaptic plasticity—changes in the strength of chemical synapses—can occur in the brain. LTP is the process of synaptic strengthening that occurs over time between pre- and postsynaptic neuronal connections. The synaptic strengthening of LTP works in opposition to the synaptic weakening of long-term depression (LTD) and together are the main mechanisms that underlie learning and memory.
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Long-term Potentiation01:25

Long-term Potentiation

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Long-term potentiation, or LTP, is one of the ways by which synaptic plasticity—changes in the strength of chemical synapses—can occur in the brain. LTP is the process of synaptic strengthening that occurs over time between pre and postsynaptic neuronal connections. The synaptic strengthening of LTP works in opposition to the synaptic weakening of long-term depression (LTD) and together are the main mechanisms that underlie learning and memory.
Hebbian LTP
LTP can occur when...
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Related Experiment Video

Updated: Apr 15, 2026

Detection of Protein Palmitoylation in Cultured Hippocampal Neurons by Immunoprecipitation and Acyl-Biotin Exchange ABE
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Postsynaptic nanodomains generated by local palmitoylation cycles.

Masaki Fukata1, Atsushi Sekiya1, Tatsuro Murakami1

  • 1*Division of Membrane Physiology, Department of Cell Physiology, National Institute for Physiological Sciences, National Institutes of Natural Sciences; and Department of Physiological Sciences, School of Life Science, SOKENDAI (the Graduate University for Advanced Studies), Okazaki 444-8787, Japan.

Biochemical Society Transactions
|April 8, 2015
PubMed
Summary

Protein palmitoylation, a key modification, drives the formation of specialized membrane domains. This process is crucial for organizing proteins like PSD-95 at the synapse, enabling essential cellular functions.

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Acyl-PEGyl Exchange Gel Shift Assay for Quantitative Determination of Palmitoylation of Brain Membrane Proteins
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Imaging pHluorin-tagged Receptor Insertion to the Plasma Membrane in Primary Cultured Mouse Neurons
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Related Experiment Videos

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Detection of Protein Palmitoylation in Cultured Hippocampal Neurons by Immunoprecipitation and Acyl-Biotin Exchange ABE
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Acyl-PEGyl Exchange Gel Shift Assay for Quantitative Determination of Palmitoylation of Brain Membrane Proteins
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Imaging pHluorin-tagged Receptor Insertion to the Plasma Membrane in Primary Cultured Mouse Neurons
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Area of Science:

  • Cell Biology
  • Neuroscience
  • Biochemistry

Background:

  • Precise protein assembly at membrane domains is vital for cellular functions like synaptic transmission.
  • Mechanisms initiating and controlling protein clustering at the plasma membrane remain incompletely understood.

Purpose of the Study:

  • This review focuses on the role of protein palmitoylation in regulating protein assembly at specialized membrane domains.
  • It specifically examines the palmitoylation of PSD-95 and its role in postsynaptic nanodomain formation.

Main Methods:

  • The review synthesizes existing research on protein palmitoylation and its impact on membrane protein organization.
  • It discusses the functional consequences of palmitoylation-dependent protein clustering.

Main Results:

  • Protein palmitoylation is a critical post-translational modification that directs proteins to specialized membrane domains.
  • Palmitoylation of PSD-95 is essential for creating discrete postsynaptic nanodomains.
  • Local palmitoylation cycles generate hotspots for protein concentration, organizing functional membrane domains.

Conclusions:

  • Palmitoylation is a key regulator of protein clustering and functional domain organization at the plasma membrane.
  • Understanding these palmitoylation cycles provides insights into synaptic function and potential therapeutic targets.