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Characterization of the zinc finger proteins ZMYM2 and ZMYM4 as novel B-MYB binding proteins
B-MYB, a highly conserved member of the MYB transcription factor family, is expressed ubiquitously in proliferating cells and plays key roles in important cell cycle-related processes, such as control of G2/M-phase transcription, cytokinesis, G1/S-phase progression and DNA-damage reponse. Deregulati...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7242444/ https://www.ncbi.nlm.nih.gov/pubmed/32439918 http://dx.doi.org/10.1038/s41598-020-65443-w |
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author | Cibis, Hannah Biyanee, Abhiruchi Dörner, Wolfgang Mootz, Henning D. Klempnauer, Karl-Heinz |
author_facet | Cibis, Hannah Biyanee, Abhiruchi Dörner, Wolfgang Mootz, Henning D. Klempnauer, Karl-Heinz |
author_sort | Cibis, Hannah |
collection | PubMed |
description | B-MYB, a highly conserved member of the MYB transcription factor family, is expressed ubiquitously in proliferating cells and plays key roles in important cell cycle-related processes, such as control of G2/M-phase transcription, cytokinesis, G1/S-phase progression and DNA-damage reponse. Deregulation of B-MYB function is characteristic of several types of tumor cells, underlining its oncogenic potential. To gain a better understanding of the functions of B-MYB we have employed affinity purification coupled to mass spectrometry to discover novel B-MYB interacting proteins. Here we have identified the zinc-finger proteins ZMYM2 and ZMYM4 as novel B-MYB binding proteins. ZMYM4 is a poorly studied protein whose initial characterization reported here shows that it is highly SUMOylated and that its interaction with B-MYB is stimulated upon induction of DNA damage. Unlike knockdown of B-MYB, which causes G2/M arrest and defective cytokinesis in HEK293 cells, knockdown of ZMYM2 or ZMYM4 have no obvious effects on the cell cycle of these cells. By contrast, knockdown of ZMYM2 strongly impaired the G1/S-phase progression of HepG2 cells, suggesting that ZMYM2, like B-MYB, is required for entry into S-phase in these cells. Overall, our work identifies two novel B-MYB binding partners with possible functions in the DNA-damage response and the G1/S-transition. |
format | Online Article Text |
id | pubmed-7242444 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-72424442020-05-30 Characterization of the zinc finger proteins ZMYM2 and ZMYM4 as novel B-MYB binding proteins Cibis, Hannah Biyanee, Abhiruchi Dörner, Wolfgang Mootz, Henning D. Klempnauer, Karl-Heinz Sci Rep Article B-MYB, a highly conserved member of the MYB transcription factor family, is expressed ubiquitously in proliferating cells and plays key roles in important cell cycle-related processes, such as control of G2/M-phase transcription, cytokinesis, G1/S-phase progression and DNA-damage reponse. Deregulation of B-MYB function is characteristic of several types of tumor cells, underlining its oncogenic potential. To gain a better understanding of the functions of B-MYB we have employed affinity purification coupled to mass spectrometry to discover novel B-MYB interacting proteins. Here we have identified the zinc-finger proteins ZMYM2 and ZMYM4 as novel B-MYB binding proteins. ZMYM4 is a poorly studied protein whose initial characterization reported here shows that it is highly SUMOylated and that its interaction with B-MYB is stimulated upon induction of DNA damage. Unlike knockdown of B-MYB, which causes G2/M arrest and defective cytokinesis in HEK293 cells, knockdown of ZMYM2 or ZMYM4 have no obvious effects on the cell cycle of these cells. By contrast, knockdown of ZMYM2 strongly impaired the G1/S-phase progression of HepG2 cells, suggesting that ZMYM2, like B-MYB, is required for entry into S-phase in these cells. Overall, our work identifies two novel B-MYB binding partners with possible functions in the DNA-damage response and the G1/S-transition. Nature Publishing Group UK 2020-05-21 /pmc/articles/PMC7242444/ /pubmed/32439918 http://dx.doi.org/10.1038/s41598-020-65443-w Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Cibis, Hannah Biyanee, Abhiruchi Dörner, Wolfgang Mootz, Henning D. Klempnauer, Karl-Heinz Characterization of the zinc finger proteins ZMYM2 and ZMYM4 as novel B-MYB binding proteins |
title | Characterization of the zinc finger proteins ZMYM2 and ZMYM4 as novel B-MYB binding proteins |
title_full | Characterization of the zinc finger proteins ZMYM2 and ZMYM4 as novel B-MYB binding proteins |
title_fullStr | Characterization of the zinc finger proteins ZMYM2 and ZMYM4 as novel B-MYB binding proteins |
title_full_unstemmed | Characterization of the zinc finger proteins ZMYM2 and ZMYM4 as novel B-MYB binding proteins |
title_short | Characterization of the zinc finger proteins ZMYM2 and ZMYM4 as novel B-MYB binding proteins |
title_sort | characterization of the zinc finger proteins zmym2 and zmym4 as novel b-myb binding proteins |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7242444/ https://www.ncbi.nlm.nih.gov/pubmed/32439918 http://dx.doi.org/10.1038/s41598-020-65443-w |
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