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Phosphorylation01:02

Phosphorylation

53.9K
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...
53.9K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

15.1K
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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4.5K
Feedback Inhibition00:46

Feedback Inhibition

57.1K
Biochemical reactions are occurring constantly in cells, converting starting substances to different products, usually with the help of enzymes that speed the reactions. Without enzymes, it would take far too long for most reactions to occur to be useful to the cell!
57.1K
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

5.6K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

15.1K
The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
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Related Experiment Video

Updated: Feb 3, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

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Src kinase phosphorylates Notch1 to inhibit MAML binding.

Bryce LaFoya1, Jordan A Munroe2, Xinzhu Pu3

  • 1Biomolecular Sciences PhD Program, Boise State University, Boise, ID, 83725, USA.

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|October 21, 2018
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Summary

Src family kinases (SFKs) regulate Notch signaling by phosphorylating the Notch intracellular domain (NICD). This interaction, influenced by integrins and extracellular matrix, impacts Notch-mediated transcription and protein stability.

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Notch signaling is crucial for development and disease, involving intercellular communication.
  • Integrins and extracellular matrix (ECM) are implicated in regulating Notch signaling, but mechanisms remain unclear.

Purpose of the Study:

  • To elucidate the mechanistic basis of integrin and ECM regulation of Notch signaling.
  • To identify the role of Src family kinases (SFKs) in this regulatory pathway.

Main Methods:

  • Co-immunoprecipitation to identify protein interactions.
  • Site-directed mutagenesis to study phosphorylation effects.
  • Western blotting and reporter assays to assess Notch activity and protein stability.

Main Results:

  • Src family kinases (SFKs), particularly c-Src, physically interact with the Notch intracellular domain (NICD).
  • c-Src directly phosphorylates NICD at specific tyrosine residues, enhancing Notch transcriptional activity.
  • Phosphorylation by SFKs attenuates Notch signaling by reducing MAML recruitment and decreasing NICD half-life.

Conclusions:

  • SFKs act downstream of integrins to mediate the effects of integrins and ECM on Notch signaling.
  • This study reveals a novel mechanism by which extracellular cues modulate Notch pathway activity.
  • These findings highlight Notch signaling's role as a sensor of the extracellular environment.