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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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Phosphorylation01:02

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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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Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

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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.
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Transducer Mechanism: Enzyme-Linked Receptors01:27

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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.
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Amplifying Signals via Enzymatic Cascade01:22

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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...
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Regulation and activity of the phosphatase SHP2: SH2 domains, dephosphorylation activity, and beyond.

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Updated: Aug 26, 2025

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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Emerging insights into serine/threonine-specific phosphoprotein phosphatase function and selectivity.

Thomas Kokot1,2, Maja Köhn1,2

  • 1Signalling Research Centres BIOSS and CIBSS, University of Freiburg, Freiburg 79104, Germany.

Journal of Cell Science
|October 7, 2022
PubMed
Summary

Phosphoprotein phosphatases (PPPs) regulate cellular functions by removing phosphate groups. Recent advances in proteomics and structural biology enhance understanding of PPP holoenzyme regulation and substrate specificity.

Keywords:
DephosphorylationHoloenzymePhosphatasePhosphoproteomicsSubstrate specificity

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • Protein phosphorylation is a key post-translational modification regulating protein function.
  • Phosphoprotein phosphatases (PPPs) are crucial enzymes that reverse phosphorylation, impacting numerous cellular processes.
  • PPPs function as holoenzymes, comprising catalytic and regulatory subunits, to achieve substrate specificity.

Purpose of the Study:

  • To review recent advancements in understanding the mechanisms of PPP holoenzyme regulation.
  • To provide insights into the substrate selectivity of PPPs.
  • To highlight novel approaches in studying PPP biology.

Main Methods:

  • Phosphoproteomics
  • Structural biology
  • Computational biology

Main Results:

  • Recent experimental and computational studies have significantly improved our understanding of PPP mechanisms.
  • New insights into how PPP holoenzyme composition dictates substrate binding and dephosphorylation.
  • Identification of key regulatory mechanisms governing PPP activity and specificity.

Conclusions:

  • The complex regulation of PPP holoenzymes is critical for cellular homeostasis.
  • Further research into PPPs will uncover new therapeutic targets for diseases associated with dysregulated phosphorylation.
  • Integrating multi-omics and structural data is essential for deciphering PPP function.