报告题目: Crosstalk between neddylation and ubiquitylation mediated by inositol polyphosphates: the missing link in signal-dependent CRL activation

报告人: 饶枫，南方科技大学生物系副教授

主持人:  翁杰敏 教授

报告时间: 11月28日 13:30 （周一）

报告地点: 天美娱乐534报告厅

 

报告人简介：

2016/07- 南方科技大学生物系， 副教授

2015-2016 北京生命科学研究所🫙，研究员

2011-2015 美国约翰霍普金斯大学医天美🪽，博士后 （导师: Solomon Snyder教授）

2007-2011 新加坡南洋理工大学博士（导师: Liang Zhao-Xun 教授）

2006-2007 新加坡南洋理工大学，项目主任

2001-2005 新加坡国立大学生物医学学士

 

报告内容：The Cullin-Ring E3 ubiquitin ligases (CRL) ubiquitylates a large number of proteins, yet their upstream stimuli remain largely unknown. CRL requires neddylation for optimal function and are tightly regulated by binding to the deneddylase COP9 signalosome (CSN). Elucidating the mechanism of assembly and dis-assembly of the CRL-CSN complexes is therefore key to understand CRL physiology. We found that the small molecule inositol hexakisphosphate (IP6) is an inter-molecular “bridge” mediating CRL-CSN assembly, the structural basis of which is also recently elucidated. Together with our earlier finding that IP6 kinase 1 metabolizes IP6 to trigger dis-assembly of CRL4-CSN complexes, these data suggest that IP6 and its metabolizing enzymes instill dynamics to CRL-CSN complexes. Consistent with this notion, we found that UV radiation activates CRL4 activity via post-translational modifications on IP6 kinase 1. Therefore, the inositol phosphate metabolic system sets CRL regulation in physiological contexts. 

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