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Related Concept Videos

Phosphorylation01:02

Phosphorylation

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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...
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Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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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...
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Calmodulin-dependent Signaling01:16

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Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
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Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

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When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
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Oligopeptide Competition Assay for Phosphorylation Site Determination
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Long-term dynamics of multisite phosphorylation.

Boris Y Rubinstein1, Henry H Mattingly2, Alexander M Berezhkovskii3

  • 1Stowers Institute for Medical Research, Kansas City, MO 64110.

Molecular Biology of the Cell
|May 27, 2016
PubMed
Summary
This summary is machine-generated.

Mathematical models of multisite phosphorylation, including all forms and processivity levels, reveal new dynamics. This minimal model of extracellular signal-related kinase regulation generates oscillations and bistability, advancing cell regulation understanding.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Systems Biology
  • Cellular Regulation

Background:

  • Multisite phosphorylation is crucial for cell regulation, but current models often oversimplify distinct phosphorylated forms and reaction kinetics.
  • Predictive understanding of protein phosphorylation requires sophisticated mathematical models that capture complex network dynamics.

Purpose of the Study:

  • To develop and analyze a minimal mathematical model of multisite phosphorylation that incorporates all essential intermediate forms and arbitrary reaction processivity.
  • To explore the dynamic behaviors, including bistability and oscillations, arising from a more comprehensive model of extracellular signal-related kinase (ERK) regulation.

Main Methods:

  • Development of a minimal mathematical model for multisite phosphorylation dynamics.
  • Inclusion of all partially phosphorylated species and variable reaction processivity (number of enzyme-substrate binding events).
  • Analysis of model dynamics, focusing on emergent behaviors like bistability and oscillations.

Main Results:

  • The model demonstrates that multisite phosphorylation networks, when considering all forms and arbitrary processivity, can exhibit complex dynamics beyond simple distributive or processive regimes.
  • Periodic oscillations were identified as a possible dynamic behavior in addition to bistability, which is commonly observed in simpler models.
  • Both bistability and oscillations can be achieved even at high levels of reaction processivity.

Conclusions:

  • A generalized mathematical framework for analyzing multisite phosphorylation dynamics is presented, accounting for all intermediate phosphorylated states and varying processivity.
  • The findings suggest that a more detailed mechanistic understanding of phosphorylation cycles can reveal novel regulatory mechanisms like oscillations, crucial for cellular control.
  • This work provides a foundation for more accurate predictions of cellular responses to genetic or pharmacological interventions affecting protein phosphorylation.