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北海道支部について

特別講演会のお知らせ【2019.12.9 Prof. James G. Omichinski】(2019.11.26更新)

演題

“Structural studies to define the role that phosphorylation and acetylation play in regulating key SUMO-SIM interactions required for PML-nuclear body formation”

演者

Prof. James G. Omichinski

所属

カナダ・モントリオール大学医学部 生化学&分子医学部門

日時

2019年12月9日 (月) 13:30 ~

場所

北海道大学 理学部本館N-308室

共催

生命分子化学セミナー,日本生化学会北海道支部,北海道大学物質科学フロンティアを開拓するAmbitiousリーダープログラム,フロンティア化学教育研究センター

概要

The interactions between SUMO-family proteins and SUMO-Interacting Motif (SIM) in nuclear bodies formed by the promyelocytic leukemia (PML) protein (PML-NBs) have been shown to be modulated by both phosphorylation SIM-containing proteins and acetylation of SUMO proteins. Given the potential role that these post-translational modifications play in regulating SUMO/SIM interactions in PML-NBs, we have characterized the interactions between the phosphorylated SIMs of key proteins found in PML-NBs and acetylated variants of SUMO1 using a combination of biophysical and X-ray crystallography studies. Our results demonstrate that SUMO-SIM interaction can be fine-tuned by discrete acetylation and/or phosphorylation events targeting either SUMO proteins or SIM-containing proteins to regulate protein transit in and out of PML-NBs.
In addition, the structures of the complexes suggest that there is considerable plasticity at the SUMO-SIM binding interface and this would provide for a robust mechanism to regulate proteins that transit in and out of PML-NB using various combinations of signaling mechanisms that function to regulate phosphorylation and acetylation of these factors.

連絡先

北海道大学大学院理学研究院化学部門 生物化学研究室 
 札幌市北区北10条西8丁目
 坂口 和靖
 kazuyasu@sci.hokudai.ac.jp
 011-706-2698

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