Flipping ATP to AMPlify Kinase Functions

Joshua B Sheetz; Mark A Lemmon

doi:10.1016/j.cell.2018.10.011

Flipping ATP to AMPlify Kinase Functions

Cell. 2018 Oct 18;175(3):641-642. doi: 10.1016/j.cell.2018.10.011.

Authors

Joshua B Sheetz¹, Mark A Lemmon²

Affiliations

¹ Department of Pharmacology, Yale University School of Medicine, New Haven, CT 06520, USA; Cancer Biology Institute, Yale University, West Haven, CT 06516, USA.
² Department of Pharmacology, Yale University School of Medicine, New Haven, CT 06520, USA; Cancer Biology Institute, Yale University, West Haven, CT 06516, USA. Electronic address: mark.lemmon@yale.edu.

Abstract

Understanding protein kinase family members that lack key catalytic residues-or pseudokinases-is a major challenge in cell signaling. In this issue of Cell, Sreelatha et al. (2018) describe how one pseudokinase transfers adenosine monophosphate (AMP) rather than phosphate to protein substrates, revealing unexpected catalytic diversity for the kinase fold.

Publication types

Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Comment

MeSH terms

Adenosine Triphosphate
Protein Kinases*
Proteolysis
Signal Transduction*

Substances

Adenosine Triphosphate
Protein Kinases

Grants and funding

R35 GM122485/GM/NIGMS NIH HHS/United States