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Related Concept Videos

Phosphorylation01:02

Phosphorylation

50.3K
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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Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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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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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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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....
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A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes
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A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes

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Post-translational modification-centric base editor screens to assess phosphorylation site functionality in high

Patrick H Kennedy1,2,3, Amin Alborzian Deh Sheikh1,2,3, Matthew Balakar4

  • 1Laboratory for Immunochemical Circuits, La Jolla Institute for Immunology, La Jolla, CA, USA.

Nature Methods
|April 29, 2024
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Summary

Scientists developed a new method to study thousands of dynamic post-translational modifications (PTMs) and their role in gene expression. This approach reveals previously unknown phosphorylation sites that fine-tune cellular signaling pathways.

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Area of Science:

  • Molecular Biology
  • Cellular Signaling
  • Genomics

Background:

  • Cellular functions are orchestrated by thousands of dynamic post-translational modifications (PTMs), yet technologies to link these modifications to genetic circuits at scale are limited.
  • Current understanding of signaling pathways often focuses on a limited number of key phosphorylation and transcriptional events, overlooking the complexity of PTMs.

Purpose of the Study:

  • To develop a high-throughput method for assessing the functional impact of phosphorylation sites on cellular processes.
  • To investigate the role of unstudied phosphorylation sites in T-cell activation and transcriptional modulation.

Main Methods:

  • Development of PTM-centric base editing coupled with phenotypic screening.
  • Application of temporally resolved phosphoproteomics to direct functional assessments.
  • Utilized T-cell activation as a model system to study signaling pathways.

Main Results:

  • Identified hundreds of previously unstudied phosphorylation sites that modulate Nuclear Factor of Activated T-cells (NFAT) transcriptional activity.
  • Discovered that phosphorylation mediates the nuclear localization of PHLPP1, influencing both NFAT and Nuclear Factor kappa B (NFκB) activity.
  • Demonstrated that specific phosphosite mutations can subtly alter gene expression patterns, indicating a capacity for fine-tuning transcriptional responses.

Conclusions:

  • Base editor screening of PTM sites offers a powerful platform for dissecting the functional roles of post-translational modifications within complex signaling pathways.
  • The findings highlight the significant, yet often unappreciated, contribution of numerous phosphorylation events to cellular regulation and gene expression.