A new chemical probe for phosphatidylinositol kinase activity

Chembiochem. 2014 Jun 16;15(9):1253-6. doi: 10.1002/cbic.201402155. Epub 2014 May 21.


Phosphatidylinositol kinases (PIKs) are key enzymatic regulators of membrane phospholipids and membrane environments that control many aspects of cellular function, from signal transduction to secretion, through the Golgi apparatus. Here, we have developed a photoreactive "clickable" probe, PIK-BPyne, to report the activity of PIKs. We investigated the selectivity and efficiency of the probe to both inhibit and label PIKs, and we compared PIK-BPyne to a wortmannin activity-based probe also known to target PIKs. We found that PIK-BPyne can act as an effective in situ activity-based probe, and for the first time, report changes in PI4K-IIIβ activity induced by the hepatitis C virus. These results establish the utility of PIK-BPyne for activity-based protein profiling studies of PIK function in native biological systems.

Keywords: HCV; activity-based protein profiling; enzyme activity; phosphatidylinositol kinases; photo-crosslinking.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkynes / chemistry
  • Alkynes / pharmacology*
  • Benzophenones / chemistry
  • Benzophenones / pharmacology*
  • Dose-Response Relationship, Drug
  • Enzyme Activation / drug effects
  • Fluorescent Dyes / chemistry
  • Fluorescent Dyes / pharmacology*
  • HEK293 Cells
  • Humans
  • Molecular Structure
  • Phosphotransferases (Alcohol Group Acceptor) / antagonists & inhibitors*
  • Phosphotransferases (Alcohol Group Acceptor) / metabolism
  • Structure-Activity Relationship


  • Alkynes
  • Benzophenones
  • Fluorescent Dyes
  • benzophenone
  • Phosphotransferases (Alcohol Group Acceptor)