Article ID Journal Published Year Pages File Type
2049736 FEBS Letters 2008 7 Pages PDF
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 summaryMINT-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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