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Long-term Potentiation

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 Potentiation

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.

Regulated Protein Degradation

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...

Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.

Neuroplasticity

Neuroplasticity

Neuroplasticity reflects the brain's remarkable capacity to adapt and evolve, responding dynamically to learning, experiences, or injury by reorganizing its neural circuitry. This reorganization involves creating new neural connections and refining old ones through a series of biological processes that contribute to the brain's lifelong development and adaptability.

The Proteasome

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...

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Related Experiment Video

Updated: Jun 11, 2026

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

Published on: July 25, 2019

Ubiquitination in postsynaptic function and plasticity.

Angela M Mabb¹, Michael D Ehlers

¹Department of Neurobiology, Duke University Medical Center, Durham, North Carolina 27710, USA.

Annual Review of Cell and Developmental Biology

|July 8, 2010

Summary

This summary is machine-generated.

Ubiquitination, a key protein modification, regulates synapse function and plasticity in the brain. This process is crucial for learning, memory, and brain development, impacting neuronal physiology and disorders.

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Area of Science:

Neuroscience
Cell Biology
Molecular Biology

Background:

Neurons transmit information via synapses, requiring constant network remodeling for brain functions like learning and memory.
Synaptic remodeling involves synapse formation/elimination, protein turnover, and transmission changes.
Posttranslational modification via the ubiquitin pathway at the postsynaptic membrane is an emerging regulatory mechanism.

Purpose of the Study:

To review recent findings on the role of ubiquitination and protein degradation in postsynaptic function and plasticity.
To describe postsynaptic ubiquitination pathways.
To highlight the involvement of these pathways in brain development, neuronal physiology, and brain disorders.

Main Methods:

Literature review of recent findings.
Discussion of established and emerging ubiquitination pathways.
Analysis of the impact on neuronal function and disease.

Main Results:

Ubiquitination and protein degradation are implicated in regulating postsynaptic function and plasticity.
Specific postsynaptic ubiquitination pathways have been identified.
These pathways play critical roles in brain development and neuronal physiology.

Conclusions:

Ubiquitination is a vital mechanism for synaptic plasticity and function.
Dysregulation of postsynaptic ubiquitination pathways contributes to brain disorders.
Further research into these pathways can inform therapeutic strategies for neurological conditions.