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Related Concept Videos

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...
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:
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...
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...
Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...

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Updated: May 19, 2026

Assessment of Resistance to Tyrosine Kinase Inhibitors by an Interrogation of Signal Transduction Pathways by Antibody Arrays
07:42

Assessment of Resistance to Tyrosine Kinase Inhibitors by an Interrogation of Signal Transduction Pathways by Antibody Arrays

Published on: September 19, 2018

Bacterial tyrosine kinases: evolution, biological function and structural insights.

Christophe Grangeasse1, Sylvie Nessler, Ivan Mijakovic

  • 1Bases Moléculaires et Structurales des Systèmes Infectieux, IBCP, CNRS, Université de Lyon, UMR 5086, 7 passage du Vercors, 69367 Lyon, France. c.grangeasse@ibcp.fr

Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
|August 15, 2012
PubMed
Summary
This summary is machine-generated.

Bacterial tyrosine kinases (BY-kinases) uniquely regulate essential cellular processes using a distinct ATP/GTP-binding mechanism. These enzymes are widespread in bacteria and crucial for understanding bacterial physiology and signaling.

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Assessment of Resistance to Tyrosine Kinase Inhibitors by an Interrogation of Signal Transduction Pathways by Antibody Arrays
07:42

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Published on: September 19, 2018

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Development and Application of Rapamycin-regulated Tyrosine Phosphatases
06:56

Development and Application of Rapamycin-regulated Tyrosine Phosphatases

Published on: September 6, 2024

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Reversible protein phosphorylation is a key regulatory mechanism in all organisms.
  • Bacteria utilize diverse protein kinases, including serine/threonine and recently identified tyrosine kinases.
  • Tyrosine phosphorylation plays a critical role in bacterial physiology, influencing virulence, stress response, and DNA metabolism.

Purpose of the Study:

  • To review recent advancements in understanding bacterial tyrosine kinases (BY-kinases).
  • To focus on the evolutionary origins, structural features, and functional roles of BY-kinases.
  • To explore the emerging regulatory potential of BY-kinases based on phosphoproteomic data.

Main Methods:

  • Literature review of recent studies on bacterial tyrosine kinases.
  • Analysis of evolutionary relationships and structural characteristics of BY-kinases.
  • Integration of phosphoproteomic findings to infer regulatory functions.

Main Results:

  • Bacteria possess unique tyrosine kinases (BY-kinases) distinct from eukaryotic counterparts.
  • BY-kinases utilize the ATP/GTP-binding Walker motif for autophosphorylation and substrate phosphorylation.
  • These kinases are prevalent across sequenced bacterial genomes, with no known eukaryotic orthologs.
  • Phosphoproteomic studies reveal the involvement of BY-kinases in diverse cellular processes.

Conclusions:

  • BY-kinases represent a unique class of bacterial enzymes with significant regulatory roles.
  • Understanding BY-kinases offers insights into bacterial signaling, evolution, and potential therapeutic targets.
  • Further research into BY-kinases will illuminate complex bacterial physiology.