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Phosphorylation

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...

Phosphorylation

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...

Protein Kinases and Phosphatases

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 Phosphatases

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 Dynamics in Living Cells

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

Calmodulin-dependent Signaling

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...

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Related Experiment Video

Updated: May 11, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Decoding the language of phosphorylation site dynamics.

Lily A Chylek¹

¹Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA. lac269@cornell.edu

Science Signaling

|May 9, 2013

Summary

This summary is machine-generated.

B cell antigen receptor (BCR) clustering allows spleen tyrosine kinase (SYK) to compensate for other kinase losses, activating positive feedback loops crucial for immune defense signaling.

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

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

Published on: May 3, 2018

Related Experiment Videos

Last Updated: May 11, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

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

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

Published on: May 3, 2018

Area of Science:

Immunology
Cellular Signaling
Computational Biology

Background:

Immune responses rely on immunoreceptors detecting pathogens and initiating signaling cascades.
Signal initiation involves protein reorganization and receptor phosphorylation, engaging feedback loops.
B cell antigen receptor (BCR) signaling is a key process in adaptive immunity.

Purpose of the Study:

To investigate the spatial and enzymatic requirements of BCR signaling.
To evaluate the roles of different kinases in BCR signaling with and without receptor clustering.
To explore the utility of computational models in understanding immunoreceptor signaling.

Main Methods:

Combined experimental and computational approaches were utilized.
The activity of spleen tyrosine kinase (SYK) and Src-family kinases was assessed.
The impact of B cell antigen receptor (BCR) clustering on signaling pathways was examined.

Main Results:

Receptor clustering enables spleen tyrosine kinase (SYK) to compensate for the absence of Src-family kinase activity.
B cell antigen receptor (BCR) clustering facilitates the activation of a positive feedback loop by SYK.
Kinase activity and receptor organization are critical interdependent factors in BCR signaling.

Conclusions:

Spatial organization of B cell antigen receptors (BCR) is essential for efficient signal transduction.
Spleen tyrosine kinase (SYK) plays a compensatory role in BCR signaling when receptors cluster.
Computational modeling offers valuable insights into complex biomolecular interactions in immunoreceptor signaling.