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Related Concept Videos

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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Protein Kinases and Phosphatases02:54

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Phosphorylation01:02

Phosphorylation

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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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Covalently Linked Protein Regulators02:04

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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.
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The cytoskeleton is an essential cell component that plays several structural and functional roles. However, the filaments that make up the cytoskeleton cannot function independently and depend on the accessory or ancillary proteins to effectively carry out their function. Accessory proteins associate with cytoskeletal filaments and their monomers, aiding filament formation and function. They also help in the cross-communication among cytoskeletal filaments. Cytoskeletal accessory proteins are...
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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

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Co-occurring protein phosphorylation are functionally associated.

Ying Li1, Xueya Zhou2, Zichao Zhai1

  • 1Department of Biomedical Informatics, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.

Plos Computational Biology
|May 2, 2017
PubMed
Summary
This summary is machine-generated.

This study introduces a new method to find functional links between protein modifications by looking at which ones happen together. Co-occurring post-translational modifications (PTMs) are common and suggest functional relationships.

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Area of Science:

  • Biochemistry
  • Proteomics
  • Systems Biology

Background:

  • Post-translational modifications (PTMs) significantly expand proteome complexity and regulate protein functions.
  • Understanding functional interplays between PTM sites is crucial due to the growing number of identified PTMs.

Purpose of the Study:

  • To develop and apply a novel analytical strategy to explore functional relationships between PTM sites.
  • To investigate the co-occurrence of phosphorylation sites under various conditions as an indicator of functional association.

Main Methods:

  • Proposed a co-occurrence analysis strategy for PTM sites.
  • Applied the strategy to human proteome-wide phosphorylation data from 88 conditions.
  • Analyzed sequence/structural proximity, kinase specificity, biological processes, and residue co-evolution of co-occurring sites.

Main Results:

  • Co-occurring phosphorylation events are significantly more frequent than random.
  • Identified known examples of cross-talk and functional connections through co-occurrence.
  • Co-occurring sites show proximity, shared kinase regulation, similar biological roles, and conserved co-evolution.
  • Co-occurrence states are conserved in orthologous phosphosites in the mouse proteome.

Conclusions:

  • Co-occurring phosphorylation sites are functionally associated.
  • Co-occurrence analysis is a valuable complementary method for uncovering novel functional associations between PTM sites.