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Dataset to delineate changes in association between Akt1 and its interacting partners as a function of active state of Akt1 protein
Akt1 is a multi-functional protein, implicated in multiple human solid tumors. Pertaining to its key role in cell survival, Akt1 is under focus for development of targeted therapies. Functional diversity of Akt1 is a result of its interactions with other proteins; which changes with changing context...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5454128/ https://www.ncbi.nlm.nih.gov/pubmed/28603765 http://dx.doi.org/10.1016/j.dib.2017.05.040 |
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author | Gupta, Nutan Duggal, Shweta Jailkhani, Noor Chatterjee, Samrat Rao, Kanury V.S. Kumar, Ajay |
author_facet | Gupta, Nutan Duggal, Shweta Jailkhani, Noor Chatterjee, Samrat Rao, Kanury V.S. Kumar, Ajay |
author_sort | Gupta, Nutan |
collection | PubMed |
description | Akt1 is a multi-functional protein, implicated in multiple human solid tumors. Pertaining to its key role in cell survival, Akt1 is under focus for development of targeted therapies. Functional diversity of Akt1 is a result of its interactions with other proteins; which changes with changing context. This investigation was designed to capture the dynamics of Akt1 Interactome as a function of its active state. Delineating dynamic changes in association of Akt1 with its interactors could help us comprehend how it changes as a function of inhibition of its active form. Similar information on changes in Akt1 interactome as of now is not well explored. Akt1 expressing HEK293 cells were cultured in light and heavy labeled SILAC media. Normal lysine and arginine were incorporated as light labels while for heavy labeling the isotopes were 8 and 10 Da heavier. Light labeled cells represented the indigenous state of Akt1 interactome while heavy labeled cells represented Akt1 interactome in presence of its allosteric inhibitor, MK-2206. Equal number of cells from both conditions were pooled, lysed and subjected to Affinity Purification coupled to Mass Spectroscopy (AP-MS). Additionally, SILAC labeling aided in quantitative estimation of changing association of a number of proteins which were common to the two experimental conditions, with Akt1. Data are available via ProteomeXchange with identifier PXD005976. |
format | Online Article Text |
id | pubmed-5454128 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-54541282017-06-09 Dataset to delineate changes in association between Akt1 and its interacting partners as a function of active state of Akt1 protein Gupta, Nutan Duggal, Shweta Jailkhani, Noor Chatterjee, Samrat Rao, Kanury V.S. Kumar, Ajay Data Brief Data Article Akt1 is a multi-functional protein, implicated in multiple human solid tumors. Pertaining to its key role in cell survival, Akt1 is under focus for development of targeted therapies. Functional diversity of Akt1 is a result of its interactions with other proteins; which changes with changing context. This investigation was designed to capture the dynamics of Akt1 Interactome as a function of its active state. Delineating dynamic changes in association of Akt1 with its interactors could help us comprehend how it changes as a function of inhibition of its active form. Similar information on changes in Akt1 interactome as of now is not well explored. Akt1 expressing HEK293 cells were cultured in light and heavy labeled SILAC media. Normal lysine and arginine were incorporated as light labels while for heavy labeling the isotopes were 8 and 10 Da heavier. Light labeled cells represented the indigenous state of Akt1 interactome while heavy labeled cells represented Akt1 interactome in presence of its allosteric inhibitor, MK-2206. Equal number of cells from both conditions were pooled, lysed and subjected to Affinity Purification coupled to Mass Spectroscopy (AP-MS). Additionally, SILAC labeling aided in quantitative estimation of changing association of a number of proteins which were common to the two experimental conditions, with Akt1. Data are available via ProteomeXchange with identifier PXD005976. Elsevier 2017-05-25 /pmc/articles/PMC5454128/ /pubmed/28603765 http://dx.doi.org/10.1016/j.dib.2017.05.040 Text en © 2017 The Author 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 Gupta, Nutan Duggal, Shweta Jailkhani, Noor Chatterjee, Samrat Rao, Kanury V.S. Kumar, Ajay Dataset to delineate changes in association between Akt1 and its interacting partners as a function of active state of Akt1 protein |
title | Dataset to delineate changes in association between Akt1 and its interacting partners as a function of active state of Akt1 protein |
title_full | Dataset to delineate changes in association between Akt1 and its interacting partners as a function of active state of Akt1 protein |
title_fullStr | Dataset to delineate changes in association between Akt1 and its interacting partners as a function of active state of Akt1 protein |
title_full_unstemmed | Dataset to delineate changes in association between Akt1 and its interacting partners as a function of active state of Akt1 protein |
title_short | Dataset to delineate changes in association between Akt1 and its interacting partners as a function of active state of Akt1 protein |
title_sort | dataset to delineate changes in association between akt1 and its interacting partners as a function of active state of akt1 protein |
topic | Data Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5454128/ https://www.ncbi.nlm.nih.gov/pubmed/28603765 http://dx.doi.org/10.1016/j.dib.2017.05.040 |
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