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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...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2016
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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. |
format | Online Article Text |
id | pubmed-5063796 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
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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