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Related Concept Videos

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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Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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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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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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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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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....
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Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

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Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
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Updated: Jan 19, 2026

Author Spotlight: Developing Tools to Tune the Activity of Tyrosine Phosphatases
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Author Spotlight: Developing Tools to Tune the Activity of Tyrosine Phosphatases

Published on: September 6, 2024

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Optical control of protein phosphatase function.

Taylor M Courtney1, Alexander Deiters2

  • 1Department of Chemistry, University of Pittsburgh, Pittsburgh, PA, 15260, USA.

Nature Communications
|September 28, 2019
PubMed
Summary
This summary is machine-generated.

Researchers developed a light-activated protein phosphatase (dual specificity phosphatase 6 or DUSP6/MKP3) for precise biological control. This tool reveals graded regulation of ERK nuclear translocation, advancing phosphatase research.

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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

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Related Experiment Videos

Last Updated: Jan 19, 2026

Author Spotlight: Developing Tools to Tune the Activity of Tyrosine Phosphatases
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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Protein phosphatases are crucial for essential biological processes but are less understood than kinases.
  • Existing methods for studying phosphatases lack precise spatiotemporal control.
  • Optogenetic tools offer precise control over protein function in living cells.

Purpose of the Study:

  • To develop a light-activated protein phosphatase, specifically dual specificity phosphatase 6 (DUSP6/MKP3), for precise spatiotemporal control.
  • To engineer DUSP6/MKP3 using genetic code expansion for optical control of its catalytic activity and substrate interactions.
  • To investigate the role of DUSP6/MKP3 in regulating cellular signaling pathways using optogenetic approaches.

Main Methods:

  • Genetic code expansion to incorporate caged amino acids (cysteine and lysine) into DUSP6/MKP3.
  • Development of two strategies: one to control catalytic activity and another to control protein-protein interactions.
  • Application of optogenetically controlled DUSP6/MKP3 with live cell reporters to monitor ERK signaling.

Main Results:

  • Successful engineering of light-activated DUSP6/MKP3 through genetic code expansion.
  • Demonstration of optical control over both phosphatase catalytic activity and substrate binding.
  • Discovery that ERK nuclear translocation is regulated in a graded manner by DUSP6/MKP3 activity.

Conclusions:

  • Light-activated DUSP6/MKP3 provides precise spatiotemporal control over phosphatase function.
  • The developed strategies are broadly applicable for engineering other light-activated phosphatases.
  • Optogenetic control of DUSP6/MKP3 reveals graded regulation of ERK signaling, offering new insights into cellular mechanisms.