Mass spectrometry analysis of PPIP5K1 interactions and data on cell motility of PPIP5K1-deficient cells
Gayane Machkalyan,
Phan Trieu,
Darlaine Pétrin,
Terence E. Hébert,
Gregory J. Miller
Affiliations
Gayane Machkalyan
Department of Pharmacology and Therapeutics, McGill University, Montréal, Québec, Canada
Phan Trieu
Department of Pharmacology and Therapeutics, McGill University, Montréal, Québec, Canada
Darlaine Pétrin
Department of Pharmacology and Therapeutics, McGill University, Montréal, Québec, Canada
Terence E. Hébert
Department of Pharmacology and Therapeutics, McGill University, Montréal, Québec, Canada
Gregory J. Miller
Department of Pharmacology and Therapeutics, McGill University, Montréal, Québec, Canada; Department of Chemistry, The Catholic University of America, Washington, DC, USA; Corresponding author at: Department of Chemistry, The Catholic University of America, Washington, DC, USA.
Inositol pyrophosphates are cellular signals that are created by the actions of inositol kinases and are degraded by highly active inositol phosphatases. The potent actions of these phosphatases suggest these signals must be created near their sites of action. To identify sites where the inositol kinase, PPIP5K1 acts, we performed affinity purification of PPIP5K1 from HEK293 cells and analyzed these samples using mass spectrometry to identify the proteins pesent (10.1016/j.cellsig.2016.02.002) [1]. We further decreased PPIP5K1 levels in HeLa cells and treated these with PPIP5K1 siRNA. We then monitored the motility of these cells in Scratch assays.
