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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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cAMP-dependent Protein Kinase Pathways01:25

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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 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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Protein-protein Interfaces

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Electrical current is defined as the rate at which charge flows. When there is a large current present, such as that used to run a refrigerator, a large amount of charge moves through the wire in a small amount of time. If the current is small, such as that used to operate a handheld calculator, a small amount of charge moves through the circuit over a long period of time. The SI unit for current is the ampere (A), named for the French physicist André-Marie Ampère (1775–1836).
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Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach
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Current technologies to identify protein kinase substrates in high throughput.

Liang Xue1, W Andy Tao2

  • 1Department of Biochemistry, Purdue University, West Lafayette, IN 47907, USA.

Frontiers in Biology
|August 12, 2014
PubMed
Summary

Identifying protein kinase substrates is crucial for understanding diseases like cancer. This review covers high-throughput genetic and proteomic methods for this important task.

Keywords:
high throughput screeningin vitro kinase assaykinase substratemass spectrometryphosphoproteomicsphosphorylation

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • Protein phosphorylation regulates numerous cellular processes.
  • Protein kinases are implicated in major diseases including cancer, diabetes, and CNS disorders.
  • Understanding disease at the molecular level necessitates identifying kinase substrates.

Purpose of the Study:

  • To review recent high-throughput techniques for identifying protein kinase substrates.
  • To discuss the advantages and limitations of various genetic and proteomic approaches.

Main Methods:

  • Focus on high-throughput genetic methods for kinase substrate identification.
  • Focus on high-throughput proteomic methods for kinase substrate identification.

Main Results:

  • Discussion of various techniques for kinase substrate identification.
  • Analysis of the strengths and weaknesses of each method.

Conclusions:

  • Comprehensive identification of kinase substrates is essential for advancing disease research.
  • Genetic and proteomic approaches offer powerful tools for high-throughput substrate discovery.