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. 2018 Aug 18;19(8):2441. doi: 10.3390/ijms19082441

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© 2018 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Phosphorylation of nuclear YB-1 after stimulation with epidermal growth factor (EGF) is associated with nuclear accumulation of RSK1 and RSK2 but not YB-1. (A,B) KRASwt HBL-100, and MCF7 cells were treated with EGF (100 ng/mL). Cytoplasmic and nuclear fractions were isolated at the indicated time points after stimulation. (C) Total protein samples (60 µg) were extracted under untreated control condition. (D) Cells were treated with erlotinib (10 µM, 2 h) followed by EGF treatment. Cytoplasmic and nuclear protein fractions were isolated at the 10 min and 30 min time-points after EGF treatment. P-RSK, RSK1/2/3, RSK1, RSK2, RSK3, P-YB-1, YB-1 and P-Akt were detected by Western botting. α-Tubulin and lamin A/C were used as cytoplasmic and nuclear markers, respectively.

Phosphorylation of nuclear YB-1 after stimulation with epidermal growth factor (EGF) is associated with nuclear accumulation of RSK1 and RSK2 but not YB-1. (A,B) KRASwt HBL-100, and MCF7 cells were treated with EGF (100 ng/mL). Cytoplasmic and nuclear fractions were isolated at the indicated time points after stimulation. (C) Total protein samples (60 µg) were extracted under untreated control condition. (D) Cells were treated with erlotinib (10 µM, 2 h) followed by EGF treatment. Cytoplasmic and nuclear protein fractions were isolated at the 10 min and 30 min time-points after EGF treatment. P-RSK, RSK1/2/3, RSK1, RSK2, RSK3, P-YB-1, YB-1 and P-Akt were detected by Western botting. α-Tubulin and lamin A/C were used as cytoplasmic and nuclear markers, respectively.