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Related Concept Videos

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...
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:

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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

P-N bond protein phosphatases.

Paul V Attwood1

  • 1School of Biomedical, Biomolecular and Chemical Sciences (M310), The University of Western Australia, 35 Stirling Highway, Crawley, WA 6009, Australia. pattwood@cyllene.uwa.edu.au

Biochimica Et Biophysica Acta
|March 28, 2012
PubMed
Summary
This summary is machine-generated.

This review covers protein phosphorylation on arginine, lysine, and histidine residues, focusing on the poorly understood phosphatases that remove these modifications. Specificity varies, with some enzymes acting broadly and others targeting particular phosphoamino acids.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Protein phosphorylation on arginine, lysine, and histidine residues is less understood than on serine, threonine, or tyrosine.
  • While histidine phosphorylation is crucial in bacteria, plants, and fungi signaling, its role in vertebrates is unclear.
  • Protein kinases and phosphatases involved in these modifications are key targets for research.

Purpose of the Study:

  • To review current knowledge on protein arginine, lysine, and histidine phosphorylation.
  • To highlight the characterization, mechanisms, and biological roles of phosphatases acting on these residues.
  • To emphasize the limited understanding of protein phosphoarginine and phospholysine phosphatases.

Main Methods:

  • Literature review of existing research on protein phosphorylation and dephosphorylation.
  • Analysis of characterized protein phosphatases, including their substrate specificities and structures.
  • Comparison of phosphorylation mechanisms across different organisms.

Main Results:

  • Protein arginine and lysine phosphorylation and their kinases are poorly understood.
  • Protein histidine phosphorylation is vital in microbial and plant signaling, with less known in vertebrates.
  • Specific protein phosphohistidine phosphatases (e.g., bacterial SixA) are well-characterized, unlike most phosphoarginine and phospholysine phosphatases.

Conclusions:

  • Further research is needed to elucidate the roles of protein arginine, lysine, and histidine phosphorylation in cellular systems.
  • Understanding specific phosphatases is crucial for deciphering signaling pathways involving these modifications.
  • The broad substrate specificity of some phosphatases contrasts with the specific roles of others, like SixA.