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. 2021 Mar 30;10(4):759. doi: 10.3390/cells10040759

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© 2021 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 (https://creativecommons.org/licenses/by/4.0/).

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Phosphorylation of Thr326 and Ser408 was required for the nuclear translocation of SRPK1. (A) Western blot of the cell extracts prepared from HeLa cells transfected with FLAG-SRPK1, FLAG-SRPK1326A, FLAG-SRPK1408A, and FLAG-SRPK1326/408A (left panel). Phosphorylation of GST-LBRNt(62–92) by 0.5 µg wild-type GST-SRPK1, GST-SRPK1326A, GST-SRPK1408A, and GST-SRPK1326/408A (right panel). (B) Fluorescent pattern of wild-type FLAG-SRPK1, FLAG-SRPK1326A, FLAG-SRPK1408A, and FLAG-SRPK1326/408A in the control and 5-FU-treated HeLa cells. In the transfected cells, the concentration of 5-FU was raised to 40 μg/mL to achieve complete nuclear translocation of FLAG-SRPK1. SRPK1 was detected using the M5 anti-FLAG monoclonal antibody, while nuclei were stained with PI. Scale bar: 10 µM.