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. 2014 Aug 15;28(16):1758–1771. doi: 10.1101/gad.246561.114

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© 2014 Cheng et al.; Published by Cold Spring Harbor Laboratory Press

This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see http://genesdev.cshlp.org/site/misc/terms.xhtml). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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Figure 4. — Structure-guided mutations on KDM2A abolish its H3K36me2 demethylation activity in cells. (A) Overexpression of wild-type KDM2A, but not KDM2A carrying D214A or N298A mutations, reduces global H3K36me2 level in cells. Western analysis with the indicated antibodies of whole-cell extract (WCE) from 293T cells transfected with control vector, wild-type KDM2A, or catalytically inactive mutants. Total H3 is shown as loading control. (B) Depletion of KDM2A by RNAi increases global H3K36me2 level in cells. Western analysis as in A of whole-cell extract from HT1080 cells carrying control vector or stably expressing two independent RNAi targeting KDM2A transcript. (C) Complementation of KDM2A-depleted HT1080 cells with wild-type KDM2A, but not KDM2A_D214A or KDM2A_N298A, restores global H3K36me2 to the control level. Western analysis as in B of whole-cell extract from HT1080 control cells and KDM2A-depleted cells stably expressing KDM2A_WT or catalytically inactive KDM2A.