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& beta; -actin; p53; interaction; DNA damage; nuclear localization

As a tumor suppressor, p53 preserves genomic integrity in eukaryotes. However, limited evidence is availablefor the p53 shuttling between the cytoplasm and nucleus. Previous studies have shown that β-actin polymerizationnegatively regulates p53 nuclear import through its interaction with p53. In this study, we found thatDNA damage induces both b-actin and p53 accumulation in the nucleus. b-actin knockdown impaired thenuclear transport of p53. Additionally, b-actin could interact with p53 which was enhanced in response togenotoxic stress. Furthermore, N terminal deletion mutants of p53 shows reduced levels of association with β-actin.We further identified Ser15, Thr18 and Ser20 of p53 are critical to the β-actin: p53 interaction, whichupon mutation into alanine abrogates the binding. Taken together, this study reveals that β-actin regulates thenuclear import of p53 through protein–protein interaction.

WENJING QI¹ JINJIAO LI² XIAOHUA PEI¹ YUESHUANG KE² QINGPAN BU¹ XIUZHEN NI¹

1. Department of Bioscience, Changchun Normal University, 677 Changji Northroad, Changchun 130032, Jilin, China
2. The Key Laboratory of Molecular Epigenetics of MOE, Institute of Genetics and Cytology, School of Life Sciences, Northeast Normal University, Changchun 130024, Jilin, China

Published

10 February 2020