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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...
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...

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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
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Published on: April 29, 2022

Protein phosphatase 5.

Terry D Hinds1, Edwin R Sánchez

  • 1Department of Physiology & Pharmacology, University of Toledo College of Medicine, 3035 Arlington Avenue, Toledo, OH 43614-5804, USA. Terry.Hinds@utoledo.edu

The International Journal of Biochemistry & Cell Biology
|October 24, 2007
PubMed
Summary

Protein phosphatase 5 (PP5), a serine/threonine phosphatase with unique TPR domains, plays a modulatory role in diverse cellular processes. PP5 deficiency in mice highlights its non-essential but significant function in cell signaling pathways.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Protein phosphatase 5 (PP5) is a unique serine/threonine phosphatase in the PPP family.
  • PP5 possesses tetratricopeptide repeat (TPR) domains, distinguishing its structure.
  • PP5 is linked to numerous cellular functions, including growth, DNA repair, and hormone signaling.

Purpose of the Study:

  • To review the signaling involvement of PP5.
  • To correlate PP5's diverse cellular activities with its structural characteristics.
  • To discuss the implications of PP5-deficient mice on understanding its biological role.

Main Methods:

  • Literature review of recent findings on PP5 signaling.
  • Analysis of PP5's structural features, particularly TPR domains.
  • Correlation of PP5's known functions with experimental data, including studies on PP5-deficient mice.

Main Results:

  • PP5 modulates various signaling pathways, including MAPK, p53/ATM/ATR, and glucocorticoid receptor (GR) signaling.
  • The presence of TPR domains likely contributes to PP5's diverse protein interactions and regulatory functions.
  • PP5-deficient mice are viable, indicating PP5 is a modulatory rather than essential factor in phosphorylation.

Conclusions:

  • PP5's unique structure facilitates its involvement in a wide array of cellular processes.
  • The modulatory role of PP5 is crucial for fine-tuning cellular responses.
  • Further research is needed to fully elucidate the mechanisms by which PP5 exerts its effects.