Related Experiment Video

Updated: May 31, 2026

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
08:00

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

Control of genetically prescribed protein tyrosine kinase activities by environment-linked redox reactions

Izumi Nakashima1, Yoshiyuki Kawamoto, Kozue Takeda

  • 1Department of Biomedical Sciences, College of Life and Health Sciences, Chubu University, Kasugai, Aichi 487-8501, Japan.

Enzyme Research
|July 15, 2011
PubMed

Insights

Environmental redox reactions regulate cell signaling by affecting protein tyrosine kinases (PTKs). Reactive oxygen species (ROS) can alter PTK activity through phosphatases or direct cysteine oxidation, impacting cell activation and death.

Area of Science:

  • Cellular Biology
  • Biochemistry
  • Molecular Signaling

Background:

  • Cellular signaling pathways control cell activation and death.
  • Protein tyrosine kinases (PTKs) are key regulators in these signaling pathways.
  • Environmental factors can influence cellular processes.

Purpose of the Study:

  • To review how environment-linked redox reactions regulate protein tyrosine kinases (PTKs).
  • To explore the mechanisms by which reactive oxygen species (ROS) affect PTK activity.
  • To discuss the role of redox reactions in modifying protein structure and signaling.

Main Methods:

  • Literature review of recent observations on PTK regulation.
  • Analysis of the impact of redox reactions on cell surface receptors and lipid rafts.
  • Examination of ROS generation and its downstream effects on PTKs and phosphatases.

Main Results:

  • Redox reactions influence PTKs primarily through cell surface receptors and lipid rafts, generating reactive oxygen species (ROS).
  • ROS can upregulate PTK activity by inactivating protein tyrosine phosphatases.
  • ROS can also directly oxidize cysteine residues on PTKs, leading to dimerization and altered catalytic activity.

Conclusions:

  • Redox reactions play a fundamental role in modulating PTK activity, influencing cell fate.
  • The direct oxidation of PTKs by ROS offers an alternative regulatory mechanism.
  • Understanding these redox-mediated modifications is crucial for comprehending cellular signaling systems.

More Related Videos

Light-mediated Reversible Modulation of the Mitogen-activated Protein Kinase Pathway during Cell Differentiation and Xenopus Embryonic Development09:32

Light-mediated Reversible Modulation of the Mitogen-activated Protein Kinase Pathway during Cell Differentiation and Xenopus Embryonic Development

Published on: June 15, 2017

Monitoring On-Target Signaling Responses in Larval Zebrafish - Z-REX Unmasks Precise Mechanisms of Electrophilic Drugs and Metabolites05:28

Monitoring On-Target Signaling Responses in Larval Zebrafish - Z-REX Unmasks Precise Mechanisms of Electrophilic Drugs and Metabolites

Published on: June 2, 2023

Related Concept Videos

Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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.
Receptor Tyrosine Kinases01:26

Receptor Tyrosine Kinases

Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
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...
mTOR Signaling and Cancer Progression03:03

mTOR Signaling and Cancer Progression

The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
The mTOR pathway or the...
Enzyme-linked Receptors01:00

Enzyme-linked Receptors

Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...