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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...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
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...
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...

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Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins
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Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins

Published on: May 30, 2025

Profiling the tyrosine phosphorylation state using SH2 domains.

Kevin Dierck1, Kazuya Machida, Bruce J Mayer

  • 1Department of Clinical Chemistry, University Medical Center, Hamburg-Eppendorf, Germany.

Methods in Molecular Biology (Clifton, N.J.)
|February 26, 2009
PubMed
Summary

Global monitoring of cellular signaling activity is crucial for understanding disease-related pathways. This study presents novel methods for profiling tyrosine phosphorylation using Src homology 2 (SH2) domains, offering insights into cellular signaling states.

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Development and Application of Rapamycin-regulated Tyrosine Phosphatases
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Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins
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Published on: May 30, 2025

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:

  • Biochemistry and Molecular Biology
  • Cellular Signaling and Proteomics

Background:

  • Global monitoring of cellular signaling is vital for understanding biological regulation and disease mechanisms.
  • Tyrosine phosphorylation and Src homology 2 (SH2) domain interactions are critical for signal transduction.
  • SH2 domains, a large family in humans, specifically bind to phosphotyrosine sites, making them valuable probes.

Purpose of the Study:

  • To describe experimental strategies for comprehensive global profiling of cellular signaling activity using SH2 domains.
  • To enable detailed characterization of signaling pathways, particularly those deregulated in disease states.

Main Methods:

  • High-resolution phosphoproteomic scanning via far-Western Blot analysis.
  • High-throughput profiling using a novel oligonucleotide-tagged multiplex assay (OTM).
  • Profiling utilizing the developed Rosette assay.

Main Results:

  • Demonstrated the utility of SH2 domains as probes for comprehensive cellular signaling state profiling.
  • Presented distinct experimental strategies enabling both high-resolution and high-throughput SH2 profiling.
  • Established methods for analyzing tyrosine phosphorylation patterns crucial for signal transmission.

Conclusions:

  • The described SH2 profiling strategies provide powerful tools for dissecting complex cellular signaling networks.
  • These methods facilitate the identification of signaling alterations in disease contexts.
  • Global SH2 profiling offers a comprehensive approach to understanding cellular states.