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Assaying Protein Kinase Activity with Radiolabeled ATP
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Flipping ATP to AMPlify Kinase Functions.

Joshua B Sheetz1, Mark A Lemmon1

  • 1Department of Pharmacology, Yale University School of Medicine, New Haven, CT 06520, USA; Cancer Biology Institute, Yale University, West Haven, CT 06516, USA.

Cell
|October 20, 2018
PubMed
Summary

Pseudokinases, protein kinases lacking key catalytic residues, present a challenge in cell signaling. A study reveals one pseudokinase transfers adenosine monophosphate (AMP) to substrates, showing novel catalytic functions for the kinase fold.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Signaling

Background:

  • Protein kinases are crucial enzymes regulating cellular processes.
  • Pseudokinases are a subclass of protein kinases that lack essential catalytic residues.
  • Understanding pseudokinase function is vital for deciphering complex cell signaling networks.

Purpose of the Study:

  • To investigate the catalytic activity and substrate interactions of a specific pseudokinase.
  • To elucidate the mechanism by which pseudokinases deviate from canonical kinase function.
  • To reveal novel catalytic mechanisms within the broader kinase superfamily.

Main Methods:

  • Biochemical assays to measure enzyme activity.
  • Protein crystallography to determine structural details.
  • Mass spectrometry to identify protein substrates and modifications.

Main Results:

  • The studied pseudokinase was found to transfer adenosine monophosphate (AMP) instead of phosphate to protein substrates.
  • This AMP transfer activity represents a previously unrecognized catalytic function for a kinase-like enzyme.
  • Structural analysis provided insights into the altered active site accommodating this unique catalytic mechanism.

Conclusions:

  • Pseudokinases exhibit a broader catalytic repertoire than previously assumed.
  • The kinase fold can accommodate diverse catalytic activities beyond canonical phosphorylation.
  • This discovery expands our understanding of enzyme evolution and the complexity of cell signaling.