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. 2017 May 10;8(40):66987–67000. doi: 10.18632/oncotarget.17791

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Copyright: © 2017 Zhao et al.

This article is distributed under the terms of the Creative Commons Attribution License (CC-BY), which permits unrestricted use and redistribution provided that the original author and source are credited.

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(A) Co-immunoprecipitation between the plasmid-encoded AKT1 and AR in HEK293T cells using anti-Flag or anti-HA antibodies. (B) In vitro GST pull-down of AR-AKT1 (both expressed in bacteria) complex. (C) EGF treatment time dependently enhanced the AR-AKT1 interaction. (D) Constitutively-active AKT1 (HA-AKT1^T308D/S473D) had a higher affinity for AR than the WT AKT1 or constitutively inactive AKT1 (HA-AKT1^T308A/S473A). (E) AR physically interacts with the kinase domain (KD) but not the PH/helix or the RD domain of AKT1.