These authors have contributed equally to this work.
MBD5 and MBD6 interact with the human PR-DUB complex through their methyl-CpG-binding domain
Article first published online: 24 APR 2014
© 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Special Issue: Proteomics in Chromatin Biology and Epigenetics
Volume 14, Issue 19, pages 2179–2189, October 2014
How to Cite
Baymaz, H. I., Fournier, A., Laget, S., Ji, Z., Jansen, P. W. T. C., Smits, A. H., Ferry, L., Mensinga, A., Poser, I., Sharrocks, A., Defossez, P.-A. and Vermeulen, M. (2014), MBD5 and MBD6 interact with the human PR-DUB complex through their methyl-CpG-binding domain. Proteomics, 14: 2179–2189. doi: 10.1002/pmic.201400013
- Issue published online: 2 OCT 2014
- Article first published online: 24 APR 2014
- Accepted manuscript online: 13 MAR 2014 08:46AM EST
- Manuscript Accepted: 7 MAR 2014
- Manuscript Received: 17 JAN 2014
- Vermeulen and Marc Timmers's groups and Berend Snel for fruitful discussions
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|pmic7715-sup-0001-FigureS1.pdf||552K||Supplementary Figure 1A. GFP-FOXK2 interactors visualized in a volcano plot. GFP-FOXK2 interactors are localized in the right part of the figure. 1B. Validation of shRNA mediated BAP1 knock-down in GFP-MBD6 HeLa FRT cells by qPCR (left) and Western blotting (right) .|
|pmic7715-sup-0002-FigureS2.pptx||8185K||Supplementary Figure 2. Detailed kinetics of MBD6 recruitment to sites of laser-induced DNA damage. Live-cell imaging of laser-microirradiated HeLa FRT cells stably expressing GFP-MBD6 at the indicated time points.|
|pmic7715-sup-0003-TableS1.xls||9898K||Supplementary Table 1: Proteingroups output tables (Maxquant) of the SILAC and label-free based GFP affinity purifications and LC-MS/MS analyses. For the SILAC-based pull-downs (MBD5-GFP, MBD6-GFP, BAP1-GFP, ASXL2-GFP, MBDonly_MBD5-GFP, deltaMBD_MBD5-GFP), proteins are sorted according to the normalized forward SILAC ratio. For the label-free pull-down (FOXK2-GFP) according to their LFQ intensity (GFP1).|
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