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Related Concept Videos

The Proteasome01:13

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...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst 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. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
Regulated Protein Degradation02:58

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...
Role of Matrix Metalloproteases in Degradation of ECM01:23

Role of Matrix Metalloproteases in Degradation of ECM

Matrix metalloproteases (MMPs) are enzymes involved in the hydrolysis of proteins and glycoproteins of the extracellular matrix. MMPs are essential for the migration and proliferation of cells through the dense matrix network, throughout embryonic development, and throughout morphogenesis. The first MMP activity discovered was a collagenase in a tadpole's tail undergoing metamorphosis. The active collagen deposition and modifications lead to the morphogenesis of tadpoles into the adult body.
A...
The Extracellular Matrix01:42

The Extracellular Matrix

Overview
The Extracellular Matrix01:29

The Extracellular Matrix

Overview
In order to maintain tissue organization, many animal cells are surrounded by structural molecules that make up the extracellular matrix (ECM). Together, the molecules in the ECM maintain the structural integrity of tissue as well as the remarkable specific properties of certain tissues.
Composition of the Extracellular Matrix
The extracellular matrix (ECM) is commonly composed of ground substance, a gel-like fluid, fibrous components, and many structurally and functionally diverse...

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Related Experiment Video

Updated: May 10, 2026

Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain
09:25

Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain

Published on: May 21, 2019

Does extracellular proteolysis control mammalian cognition?

Hideki Tamura, Yasuyuki Ishikawa, Sadao Shiosaka

    Reviews in the Neurosciences
    |June 5, 2013
    PubMed
    Summary
    This summary is machine-generated.

    Extracellular proteases dynamically alter synaptic structure, influencing brain plasticity, learning, and memory. Researchers developed a new method to identify protease targets involved in these cognitive functions.

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    Quantitative Approaches for Scoring in vivo Neuronal Aggregate and Organelle Extrusion in Large Exopher Vesicles in C. elegans
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    Quantitative Approaches for Scoring in vivo Neuronal Aggregate and Organelle Extrusion in Large Exopher Vesicles in C. elegans

    Published on: September 18, 2020

    Area of Science:

    • Neuroscience
    • Molecular Biology
    • Cognitive Science

    Background:

    • Synaptic plasticity, crucial for learning and memory, involves dynamic structural changes in mature nervous systems.
    • Extracellular proteases are increasingly recognized for their role in modifying synaptic structure through targeted protein cleavage.

    Purpose of the Study:

    • To review molecular mechanisms of cognition-related focal proteolysis in the hippocampus.
    • To introduce a novel screening method for identifying physiological protease substrates.

    Main Methods:

    • Review of current literature on extracellular proteases and synaptic plasticity.
    • Development and description of a new screening technique for protease substrate identification.

    Main Results:

    • Extracellular proteases mediate synaptic structural modifications via limited proteolysis of key neuronal components.
    • These modifications can alter protein function or release active domains, initiating signaling cascades.
    • The proposed screening method aids in discovering novel physiological substrates for proteases.

    Conclusions:

    • Focal proteolysis in the hippocampus is a key molecular mechanism underlying cognitive functions like learning and memory.
    • The novel screening method offers a valuable tool for advancing research into protease functions in the brain.