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Data in support of DPF2 regulates OCT4 protein level and nuclear distribution
DPF2, also named ubi-d4/requiem (REQU), interacts with a protein complex containing OCT4. This paper provides data in support of the research article entitled “DPF2 regulates OCT4 protein level and nuclear distribution”. The highlights include: (1) Denature-immunoprecipitation assay revealed ubiquit...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4773415/ https://www.ncbi.nlm.nih.gov/pubmed/26958616 http://dx.doi.org/10.1016/j.dib.2015.10.010 |
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author | Liu, Chao Zhang, Dijuan Shen, Yuxian Tao, Xiaofang Liu, Lihua Zhong, Yongwang Fang, Shengyun |
author_facet | Liu, Chao Zhang, Dijuan Shen, Yuxian Tao, Xiaofang Liu, Lihua Zhong, Yongwang Fang, Shengyun |
author_sort | Liu, Chao |
collection | PubMed |
description | DPF2, also named ubi-d4/requiem (REQU), interacts with a protein complex containing OCT4. This paper provides data in support of the research article entitled “DPF2 regulates OCT4 protein level and nuclear distribution”. The highlights include: (1) Denature-immunoprecipitation assay revealed ubiquitination of OCT4 in pluripotent H9 cells, which was enhancedby MG132, a proteasome inhibitor. (2) Well colocalization of ectopic OCT4 and FLAG-Ub was found in HeLa cells, which was also increased by MG132. (3) MG132 treatment decreased DPF2 cytoplasmic expression in vivo. These data give insights into how proteasome inhibition contributes to studying ubiquitnation of OCT4. |
format | Online Article Text |
id | pubmed-4773415 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-47734152016-03-08 Data in support of DPF2 regulates OCT4 protein level and nuclear distribution Liu, Chao Zhang, Dijuan Shen, Yuxian Tao, Xiaofang Liu, Lihua Zhong, Yongwang Fang, Shengyun Data Brief Data Article DPF2, also named ubi-d4/requiem (REQU), interacts with a protein complex containing OCT4. This paper provides data in support of the research article entitled “DPF2 regulates OCT4 protein level and nuclear distribution”. The highlights include: (1) Denature-immunoprecipitation assay revealed ubiquitination of OCT4 in pluripotent H9 cells, which was enhancedby MG132, a proteasome inhibitor. (2) Well colocalization of ectopic OCT4 and FLAG-Ub was found in HeLa cells, which was also increased by MG132. (3) MG132 treatment decreased DPF2 cytoplasmic expression in vivo. These data give insights into how proteasome inhibition contributes to studying ubiquitnation of OCT4. Elsevier 2015-10-19 /pmc/articles/PMC4773415/ /pubmed/26958616 http://dx.doi.org/10.1016/j.dib.2015.10.010 Text en © 2015 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 Liu, Chao Zhang, Dijuan Shen, Yuxian Tao, Xiaofang Liu, Lihua Zhong, Yongwang Fang, Shengyun Data in support of DPF2 regulates OCT4 protein level and nuclear distribution |
title | Data in support of DPF2 regulates OCT4 protein level and nuclear distribution |
title_full | Data in support of DPF2 regulates OCT4 protein level and nuclear distribution |
title_fullStr | Data in support of DPF2 regulates OCT4 protein level and nuclear distribution |
title_full_unstemmed | Data in support of DPF2 regulates OCT4 protein level and nuclear distribution |
title_short | Data in support of DPF2 regulates OCT4 protein level and nuclear distribution |
title_sort | data in support of dpf2 regulates oct4 protein level and nuclear distribution |
topic | Data Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4773415/ https://www.ncbi.nlm.nih.gov/pubmed/26958616 http://dx.doi.org/10.1016/j.dib.2015.10.010 |
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