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

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 ki...

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Autores principales: Machkalyan, Gayane, Trieu, Phan, Pétrin, Darlaine, Hébert, Terence E., Miller, Gregory J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5063796/
https://www.ncbi.nlm.nih.gov/pubmed/27761507
http://dx.doi.org/10.1016/j.dib.2016.03.035
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author Machkalyan, Gayane
Trieu, Phan
Pétrin, Darlaine
Hébert, Terence E.
Miller, Gregory J.
author_facet Machkalyan, Gayane
Trieu, Phan
Pétrin, Darlaine
Hébert, Terence E.
Miller, Gregory J.
author_sort Machkalyan, Gayane
collection PubMed
description 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.
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spelling pubmed-50637962016-10-19 Mass spectrometry analysis of PPIP5K1 interactions and data on cell motility of PPIP5K1-deficient cells Machkalyan, Gayane Trieu, Phan Pétrin, Darlaine Hébert, Terence E. Miller, Gregory J. Data Brief Data Article 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. Elsevier 2016-04-02 /pmc/articles/PMC5063796/ /pubmed/27761507 http://dx.doi.org/10.1016/j.dib.2016.03.035 Text en © 2016 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Data Article
Machkalyan, Gayane
Trieu, Phan
Pétrin, Darlaine
Hébert, Terence E.
Miller, Gregory J.
Mass spectrometry analysis of PPIP5K1 interactions and data on cell motility of PPIP5K1-deficient cells
title Mass spectrometry analysis of PPIP5K1 interactions and data on cell motility of PPIP5K1-deficient cells
title_full Mass spectrometry analysis of PPIP5K1 interactions and data on cell motility of PPIP5K1-deficient cells
title_fullStr Mass spectrometry analysis of PPIP5K1 interactions and data on cell motility of PPIP5K1-deficient cells
title_full_unstemmed Mass spectrometry analysis of PPIP5K1 interactions and data on cell motility of PPIP5K1-deficient cells
title_short Mass spectrometry analysis of PPIP5K1 interactions and data on cell motility of PPIP5K1-deficient cells
title_sort mass spectrometry analysis of ppip5k1 interactions and data on cell motility of ppip5k1-deficient cells
topic Data Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5063796/
https://www.ncbi.nlm.nih.gov/pubmed/27761507
http://dx.doi.org/10.1016/j.dib.2016.03.035
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