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. 2017 Nov 13;45(22):12862–12876. doi: 10.1093/nar/gkx1102

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© The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 6. — RBM45 competes with HDAC1 for binding with FUS. (A) RBM45 interacts with HDAC1. After transfected with the indicated plasmids, cells were lysed and immunoprecipitated by antibodies against HA or IgG, and the bound proteins were analyzed by immunoblotting with anti-Flag monoclonal antibody. (B) Depletion of FUS decreases the interaction between RBM45 and HDAC1. 48 h after expressing siNC or siFUS, 293T cells were cotransfected with Flag-RBM45 and HA-HDAC1, then lysed and immunoprecipitated by anti-HA antibody. The bound proteins were analyzed by immunoblotting with anti-Flag. (C) RBM45 knockdown enhances the cooperation between FUS and HDAC1. 293T cells were transfected with siNC or siRBM45 before co-transfected with flag-FUS and HA-HDAC1. Anti-HA and anti-Flag antibodies were used for precipitation and blotting, respectively. (D) HDAC1 knockdown increases the interaction between RBM45 and FUS. 293T cells expressing siRNA were co-transfected with flag-FUS and HA-RBM45. Anti-Flag M2 beads were used for immunoprecipitation, and anti-HA antibody was used for immunoblotting.