Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Protein Networks

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

Protein Networks

Protein Networks

Interactions Between Signaling Pathways

Interactions Between Signaling Pathways

Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...

Role of Matrix Metalloproteases in Degradation of ECM

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...

The Proteasome

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...

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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Genome-scale transcriptional dynamics and environmental biosensing.

Proceedings of the National Academy of Sciences of the United States of America·2020

Same author

Proteolytic Queues at ClpXP Increase Antibiotic Tolerance.

ACS synthetic biology·2019

Same author

Crosstalk between Diverse Synthetic Protein Degradation Tags in Escherichia coli.

ACS synthetic biology·2017

Same author

The spatiotemporal system dynamics of acquired resistance in an engineered microecology.

Scientific reports·2017

Same author

Mechanisms for Differential Protein Production in Toxin-Antitoxin Systems.

Toxins·2017

Same author

Entrainment of a Bacterial Synthetic Gene Oscillator through Proteolytic Queueing.

ACS synthetic biology·2016

Search research articles

Related Experiment Video

Updated: Mar 23, 2026

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Published on: April 1, 2017

Proteolytic crosstalk in multi-protease networks.

Curtis T Ogle¹, William H Mather

¹Department of Physics, Virginia Tech, 50 West Campus Dr, Blacksburg, VA 24061-0435, USA.

Physical Biology

|April 5, 2016

Summary

This summary is machine-generated.

Cellular protein degradation involves competition for limited proteases, creating queues. This study shows that multiple proteases significantly couple cellular network dynamics, leading to protein count correlations.

More Related Videos

JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics

JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics

Published on: October 19, 2021

The Determination of Protease Specificity in Mouse Tissue Extracts by MALDI-TOF Mass Spectrometry: Manipulating PH to Cause Specificity Changes

The Determination of Protease Specificity in Mouse Tissue Extracts by MALDI-TOF Mass Spectrometry: Manipulating PH to Cause Specificity Changes

Published on: May 25, 2018

Related Experiment Videos

Last Updated: Mar 23, 2026

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Published on: April 1, 2017

JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics

JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics

Published on: October 19, 2021

The Determination of Protease Specificity in Mouse Tissue Extracts by MALDI-TOF Mass Spectrometry: Manipulating PH to Cause Specificity Changes

The Determination of Protease Specificity in Mouse Tissue Extracts by MALDI-TOF Mass Spectrometry: Manipulating PH to Cause Specificity Changes

Published on: May 25, 2018

Area of Science:

Molecular Biology
Systems Biology
Biophysics

Background:

Processive proteases like ClpXP in E. coli degrade proteins for cellular regulation.
Limited proteolytic capacity creates bottlenecks, causing proteins to compete for degradation resources.
Previous studies focused on single protease competition; the impact of multiple proteases remains unclear.

Purpose of the Study:

To theoretically investigate how competition for multiple protease classes affects cellular network dynamics.
To understand the statistical relationships between protein counts under multi-protease conditions.
To explore how substrate-protease affinities influence queueing dynamics.

Main Methods:

Theoretical modeling of cellular proteolytic networks.
Analysis of protein count correlations under varying protease competition scenarios.
Investigation of substrate-protease affinity effects on queueing dynamics.

Main Results:

Multi-protease bottlenecks substantially couple simple and complex cellular networks.
Protein queueing leads to strong positive correlations in protein counts, especially near a balance point.
Network behavior depends on relative substrate-protease affinities, potentially leading to priority queueing.

Conclusions:

Competition for multiple proteases significantly impacts cellular network dynamics and protein count correlations.
Affinity differences between substrates and proteases play a crucial role in determining queueing behavior.
The findings provide insights into the complex regulation of protein turnover in cells.