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Mass spectrometry analysis of PPIP5K1 interactions and data on cell motility of PPIP5K1-deficient cells

Authors :
Gayane Machkalyan
Phan Trieu
Darlaine Pétrin
Terence E. Hébert
Gregory J. Miller
Source :
Data in Brief, Vol 7, Iss , Pp 1443-1446 (2016)
Publication Year :
2016
Publisher :
Elsevier, 2016.

Abstract

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.

Details

Language :
English
ISSN :
23523409
Volume :
7
Issue :
1443-1446
Database :
Directory of Open Access Journals
Journal :
Data in Brief
Publication Type :
Academic Journal
Accession number :
edsdoj.6df61a75dc5f4785a95056e301e6e0af
Document Type :
article
Full Text :
https://doi.org/10.1016/j.dib.2016.03.035