Phosphorylation of LSD1 by PLK1 promotes its chromatin release during mitosis

BACKGROUND: Lysine-specific histone demethylase 1 (LSD1) modulates chromatin status through demethylation of H3K4 and H3K9. It has been demonstrated that LSD1 is hyperphosphorylated and dissociates from chromatin during mitosis. However, the molecular mechanism of LSD1 detachment is unknown. RESULTS...

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Detalles Bibliográficos
Autores principales: Peng, Bin, Shi, Ruifeng, Jiang, Weiwei, Ding, Yue-He, Dong, Meng-Qiu, Zhu, Wei-Guo, Xu, Xingzhi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2017
Materias:
Research
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5364692/
https://www.ncbi.nlm.nih.gov/pubmed/28344766
http://dx.doi.org/10.1186/s13578-017-0142-x
Descripción
Sumario:BACKGROUND: Lysine-specific histone demethylase 1 (LSD1) modulates chromatin status through demethylation of H3K4 and H3K9. It has been demonstrated that LSD1 is hyperphosphorylated and dissociates from chromatin during mitosis. However, the molecular mechanism of LSD1 detachment is unknown. RESULTS: In this report, we found that polo-like kinase 1 (PLK1) directly interacted with LSD1 and phosphorylated LSD1 at Ser-126 . Nocodazole-induced metaphase arrest promoted release of LSD1 from chromatin, and the phosphorylation-defective mutant LSD1 (S126A) failed to dissociate from chromatin upon nocodazole treatment. CONCLUSIONS: Taken together, our findings demonstrate that phosphorylation of LSD1 at Ser-126 by PLK1 promotes its release from chromatin during mitosis.

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