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A New Chemical Probe for Phosphatidylinositol Kinase Activity
Author(s) -
Sherratt Allison R.,
Nasheri Neda,
McKay Craig S.,
O'Hara Shifawn,
Hunt Ashley,
Ning Zhibin,
Figeys Daniel,
Goto Natalie K.,
Pezacki John Paul
Publication year - 2014
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201402155
Subject(s) - wortmannin , phosphatidylinositol , kinase , chemistry , signal transduction , microbiology and biotechnology , biochemistry , function (biology) , enzyme , biology
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.