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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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Bacterial Protein Maturation

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Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
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NME/NM23/NDPK and Histidine Phosphorylation.

Kevin Adam1, Jia Ning1, Jeffrey Reina1

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

International Journal of Molecular Sciences
|August 23, 2020
PubMed
Summary

Nucleoside diphosphate kinases (NDPKs), also known as NME family members, exhibit conserved protein-histidine kinase activity. Recent advancements enable better study of this crucial, yet underappreciated, cell signaling role.

Keywords:
NMEhistidine kinasephosphorylation

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • NME (Non-metastatic) proteins, or NDPKs (nucleoside diphosphate kinases), are evolutionarily conserved enzymes.
  • Initially recognized for nucleoside diphosphate kinase activity, some family members also possess protein-histidine kinase activity.
  • Studying phosphohistidine modifications has been challenging due to their instability and limited molecular tools.

Purpose of the Study:

  • To provide a comprehensive overview of the NME family and histidine phosphorylation.
  • To highlight the underappreciated protein-histidine kinase activity of NME members in human cells.
  • To summarize structural, functional, and cell signaling aspects of NME family histidine kinases.

Main Methods:

  • Review of existing literature on NME family proteins and histidine phosphorylation.
  • Discussion of recent methodological advancements for studying unstable phosphohistidine modifications.
  • Synthesis of data on NME family structure, function, and signaling pathways.

Main Results:

  • NME family members, conserved across species, possess both NDPK and protein-histidine kinase activities.
  • New experimental methods have facilitated the investigation of histidine kinase activity.
  • Growing scientific interest in NME family's role in cell signaling.

Conclusions:

  • NME family proteins play a significant role in cell signaling through histidine phosphorylation.
  • Further research is needed to fully elucidate the mechanisms and implications of NME-mediated histidine kinase activity.
  • Understanding these pathways is crucial for advancing cell biology and potentially therapeutic strategies.