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Related Concept Videos

Postsynaptic Potential (PSP)01:32

Postsynaptic Potential (PSP)

Postsynaptic potential (PSP) refers to a change in the electrical potential of a neuron when neurotransmitters released by presynaptic neurons bind to postsynaptic receptors. This potential can either be excitatory, leading to depolarization and ultimately action potential generation, or inhibitory, leading to hyperpolarization and suppression of the postsynaptic neuron.
There are two types of receptors: ionotropic and metabotropic.
The ionotropic receptor is the membrane protein that has an...
Long-term Potentiation01:25

Long-term Potentiation

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 presynaptic neurons...
Long-term Potentiation01:35

Long-term Potentiation

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.
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.

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Related Experiment Video

Updated: May 14, 2026

3D Modeling of Dendritic Spines with Synaptic Plasticity
07:13

3D Modeling of Dendritic Spines with Synaptic Plasticity

Published on: May 18, 2020

SPIN90 phosphorylation modulates spine structure and synaptic function.

In Ha Cho1, Dae Hwan Kim, Min-Jung Lee

  • 1Bio Imaging and Cell Dynamics Center, School of Life Sciences, Gwangju Institute of Science and Technology, Gwangju, Korea.

Plos One
|January 24, 2013
PubMed
Summary

SPIN90 protein phosphorylation by Src kinase is crucial for its synaptic targeting and function. This process enhances synaptic activity and spine head size in neurons, impacting postsynaptic function.

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Dendritic Spine Quantification Using an Automatic Three-Dimensional Neuron Reconstruction Software

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • Dendritic spine structure and synaptic function are critical for neuronal communication.
  • SPIN90 is a key protein involved in actin dynamics, endocytosis, and dendritic spine morphogenesis.

Purpose of the Study:

  • To investigate the role of SPIN90 phosphorylation in synaptic targeting and function.
  • To determine the kinase responsible for SPIN90 phosphorylation and its impact on postsynaptic components.

Main Methods:

  • In vitro and in vivo kinase assays to identify SPIN90 kinase.
  • Expression of SPIN90 wild-type (WT) and mutant forms in cultured hippocampal neurons.
  • Immunofluorescence microscopy to assess protein localization.
  • Biochemical assays to measure binding affinity to PSD95 and Shank.
  • Electrophysiological recordings to evaluate synaptic function.

Main Results:

  • SPIN90 is tyrosine phosphorylated by Src kinase.
  • Phosphorylated SPIN90 is targeted to dendritic spines.
  • A phospho-deficient SPIN90 mutant fails to accumulate at spines.
  • SPIN90 phosphorylation enhances binding to PSD95 and Shank.
  • Overexpression of WT or phospho-mimicking SPIN90 leads to enlarged spine heads and increased synaptic activity (amplitude and frequency).

Conclusions:

  • SPIN90 phosphorylation by Src kinase is a key regulatory mechanism for its synaptic localization.
  • Phosphorylated SPIN90 enhances postsynaptic structure and function.
  • SPIN90 plays a significant role in modulating neuronal synaptic activity through phosphorylation.