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Sox2 Uses Multiple Domains to Associate with Proteins Present in Sox2-Protein Complexes
Master regulators, such as Sox2, Oct4 and Nanog, control complex gene networks necessary for the self-renewal and pluripotency of embryonic stem cells (ESC). These master regulators associate with co-activators and co-repressors to precisely control their gene targets. Recent studies using proteomic...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
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Public Library of Science
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2980493/ https://www.ncbi.nlm.nih.gov/pubmed/21103394 http://dx.doi.org/10.1371/journal.pone.0015486 |
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author | Cox, Jesse L. Mallanna, Sunil K. Luo, Xu Rizzino, Angie |
author_facet | Cox, Jesse L. Mallanna, Sunil K. Luo, Xu Rizzino, Angie |
author_sort | Cox, Jesse L. |
collection | PubMed |
description | Master regulators, such as Sox2, Oct4 and Nanog, control complex gene networks necessary for the self-renewal and pluripotency of embryonic stem cells (ESC). These master regulators associate with co-activators and co-repressors to precisely control their gene targets. Recent studies using proteomic analysis have identified a large, diverse group of co-activators and co-repressors that associate with master regulators, including Sox2. In this report, we examined the size distribution of nuclear protein complexes containing Sox2 and its associated proteins HDAC1, Sall4 and Lin28. Interestingly, we determined that Sox2 and HDAC1 associate with protein complexes that vary greatly in size; whereas, Lin28 primarily associates with smaller complexes, and Sall4 primarily associates with larger complexes. Additionally, we examined the domains of Sox2 necessary to mediate its association with its partner proteins Sall4, HDAC1 and HDAC2. We determined that Sox2 uses multiple and distinct domains to associate with its partner proteins. We also examined the domains of Sox2 necessary to mediate its self-association, and we determined that Sox2 self-association is mediated through multiple domains. Collectively, these studies provide novel insights into how Sox2 is able to associate with a wide array of nuclear proteins that control gene transcription. |
format | Text |
id | pubmed-2980493 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-29804932010-11-22 Sox2 Uses Multiple Domains to Associate with Proteins Present in Sox2-Protein Complexes Cox, Jesse L. Mallanna, Sunil K. Luo, Xu Rizzino, Angie PLoS One Research Article Master regulators, such as Sox2, Oct4 and Nanog, control complex gene networks necessary for the self-renewal and pluripotency of embryonic stem cells (ESC). These master regulators associate with co-activators and co-repressors to precisely control their gene targets. Recent studies using proteomic analysis have identified a large, diverse group of co-activators and co-repressors that associate with master regulators, including Sox2. In this report, we examined the size distribution of nuclear protein complexes containing Sox2 and its associated proteins HDAC1, Sall4 and Lin28. Interestingly, we determined that Sox2 and HDAC1 associate with protein complexes that vary greatly in size; whereas, Lin28 primarily associates with smaller complexes, and Sall4 primarily associates with larger complexes. Additionally, we examined the domains of Sox2 necessary to mediate its association with its partner proteins Sall4, HDAC1 and HDAC2. We determined that Sox2 uses multiple and distinct domains to associate with its partner proteins. We also examined the domains of Sox2 necessary to mediate its self-association, and we determined that Sox2 self-association is mediated through multiple domains. Collectively, these studies provide novel insights into how Sox2 is able to associate with a wide array of nuclear proteins that control gene transcription. Public Library of Science 2010-11-12 /pmc/articles/PMC2980493/ /pubmed/21103394 http://dx.doi.org/10.1371/journal.pone.0015486 Text en Cox et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Cox, Jesse L. Mallanna, Sunil K. Luo, Xu Rizzino, Angie Sox2 Uses Multiple Domains to Associate with Proteins Present in Sox2-Protein Complexes |
title | Sox2 Uses Multiple Domains to Associate with Proteins Present in Sox2-Protein Complexes |
title_full | Sox2 Uses Multiple Domains to Associate with Proteins Present in Sox2-Protein Complexes |
title_fullStr | Sox2 Uses Multiple Domains to Associate with Proteins Present in Sox2-Protein Complexes |
title_full_unstemmed | Sox2 Uses Multiple Domains to Associate with Proteins Present in Sox2-Protein Complexes |
title_short | Sox2 Uses Multiple Domains to Associate with Proteins Present in Sox2-Protein Complexes |
title_sort | sox2 uses multiple domains to associate with proteins present in sox2-protein complexes |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2980493/ https://www.ncbi.nlm.nih.gov/pubmed/21103394 http://dx.doi.org/10.1371/journal.pone.0015486 |
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