Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Microtubule Instability02:17

Microtubule Instability

Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated assembly and...
Microtubule Instability02:17

Microtubule Instability

Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated assembly and...
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...

You might also read

Related Articles

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

Sort by
Same author

Translating in vitro buccal permeation to in vivo and whole‑body exposure using in silico cell‑based and physiologically-based pharmacokinetic modelling.

International journal of pharmaceutics·2026
Same author

Data derived extrapolation factors (DDEFs) for rat to human interspecies extrapolation for the HPPD inhibitor mesotrione.

Critical reviews in toxicology·2024
Same author

Decomposing diversity into measures of evenness, similarity, and richness.

Ecology and evolution·2024
Same author

Mathematical modelling of oxygen gradients in stem cell-derived liver tissue.

PloS one·2021
Same author

Pressure-driven changes to spontaneous flow in active nematic liquid crystals.

The European physical journal. E, Soft matter·2020
Same author

Multiscale modelling of drug transport and metabolism in liver spheroids.

Interface focus·2020

Related Experiment Video

Updated: Jun 24, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Structural instability in an autophosphorylating kinase switch.

Michael Grinfeld1, Steven D Webb

  • 1Department of Mathematics, University of Strathclyde, 26 Richmond Street, Glasgow G1 1XH, UK. michael@maths.strath.ac.uk

Mathematical Biosciences
|March 24, 2009
PubMed
Summary
This summary is machine-generated.

This study shows that a simple kinase model loses its bistability when protein synthesis and degradation are included. This suggests that protein turnover can disrupt stable biological states.

More Related Videos

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

Identification of Kinase-substrate Pairs Using High Throughput Screening
11:13

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

Related Experiment Videos

Last Updated: Jun 24, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

Identification of Kinase-substrate Pairs Using High Throughput Screening
11:13

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

Area of Science:

  • Biochemistry
  • Systems Biology
  • Molecular Biology

Background:

  • Kinase signaling pathways are crucial for cellular processes.
  • Bistability in biological systems allows for robust decision-making.
  • Understanding the conditions that maintain or disrupt bistability is essential.

Purpose of the Study:

  • To investigate the impact of protein turnover on the bistability of a simple kinase model.
  • To analytically determine if bistability is conserved under conditions of synthesis and degradation.

Main Methods:

  • Analysis of a simplified mathematical model of kinase activity.
  • Analytical derivation of conditions for bistability.
  • Inclusion of protein synthesis and degradation terms in the model.

Main Results:

  • The simple kinase model exhibits bistability in the absence of protein turnover.
  • Analytical results demonstrate that bistability is not always conserved when protein synthesis and degradation are considered.
  • Protein turnover can lead to the loss of the bistable property.

Conclusions:

  • Protein turnover is a critical factor that can destabilize bistable signaling motifs.
  • The presence of synthesis and degradation can alter the qualitative behavior of biological networks.
  • Further investigation into the role of protein dynamics in biological switches is warranted.