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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

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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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.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
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Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

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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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cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

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Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
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Receptor Tyrosine Kinases01:26

Receptor Tyrosine Kinases

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Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
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Related Experiment Video

Updated: Jun 19, 2025

Quantification of Bacterial Histidine Kinase Autophosphorylation Using a Nitrocellulose Binding Assay
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Quantification of Bacterial Histidine Kinase Autophosphorylation Using a Nitrocellulose Binding Assay

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Histidine Phosphorylation: Protein Kinases and Phosphatases.

Jia Ning1, Margaux Sala1, Jeffrey Reina1

  • 1Molecular and Cell Biology Laboratory, Salk Institute for Biological Studies, La Jolla, CA 92037, USA.

International Journal of Molecular Sciences
|July 27, 2024
PubMed
Summary

Phosphohistidine (pHis) is a challenging but crucial protein modification. New tools reveal its cellular roles and regulation by histidine kinases and phosphatases, impacting cancer biology.

Keywords:
NMEhistidine kinasehistidine phosphatasephosphorylation

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

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Last Updated: Jun 19, 2025

Quantification of Bacterial Histidine Kinase Autophosphorylation Using a Nitrocellulose Binding Assay
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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Phosphohistidine (pHis) is a reversible protein post-translational modification (PTM) that is difficult to study due to its acid and heat sensitivity.
  • Understanding pHis is critical as it plays roles in cellular regulation, similar to other phosphoamino acids like phosphoserine, phosphothreonine, and phosphotyrosine.

Purpose of the Study:

  • To review the current understanding of phosphohistidine's cellular functions and regulation.
  • To discuss the enzymes involved in pHis modification and their substrates.
  • To explore the potential roles of pHis in cancer and the methods used to study it.

Main Methods:

  • Identification of histidine kinases (NME1, NME2) and phosphohistidine phosphatases (PHPT1, LHPP, PGAM5).
  • Substrate identification for pHis-modifying enzymes.
  • Analysis of cellular mechanisms regulating pHis kinase and phosphatase activity.

Main Results:

  • Several enzymes controlling pHis modification and their substrates have been identified.
  • Insights into novel regulatory mechanisms mediated by pHis are emerging.
  • The dual role of pHis kinases and phosphatases as potential tumor promoters or suppressors is being investigated.

Conclusions:

  • Advancements in tools are facilitating the study of pHis biology.
  • Unraveling pHis functions in mammals will provide significant new insights into cell biology.
  • pHis modification represents a key area for future research in understanding cellular regulation and disease.