Abstract

The tumor suppressor and transcription factor p53 is a key modulator of cellular stress responses and can trigger apoptosis in many cell types, including neurons. In this study, we have shown that the Microtubule-Associated Protein 1B (MAP1B) light chain can interact with the tumor suppressor p53. We also demonstrate that both p53 and the MAP1B light chain (MAP1B-LC1) alter their localization from the cytoplasm to the nucleus when neuroblastoma cells, SH-SY5Y, are treated with doxorubicin. Additionally, we demonstrate that the MAP1B-LC1 negatively regulates p53-dependent transcriptional activity of a reporter construct driven by the p21 promoter. Consequently, MAP1B-LC1 binds to p53 and this interaction leads to the inhibition of doxorubicin-induced apoptosis in SH-SY5Y cells. Structured summary MINT- 6701342, MINT- 6706444: MAP1B- LC (uniprotkb: P46821) and P53 (uniprotkb: P04637) colocalize (MI: 0403) by fluorescence microscopy (MI: 0416) MINT- 6700861, MINT- 6701791: P53 (uniprotkb: P04637) physically interacts (MI: 0218) with MAP1B- LC (uniprotkb: P46821) by anti bait coimmunoprecipitation (MI: 0006) MINT- 6702266, MINT- 6702529: P53 (uniprotkb: P04637) physically interacts (MI: 0218) with MAP1B- LC (uniprotkb: P46821) by anti tag coimmunoprecipitation (MI: 0007)

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