报告题目

Organizations of NeuronalSynapses: a new phase of biochemistry and cell biology investigation

主讲人：张明杰

中国科学院院士

香港科学院创院院士

香港科技大学讲座教授

中国科学技术大学生命科学学院院长

时  间：2019年5月16日16:00-17:00

地  点：上海交通大学闵行校区生物药学楼树华报告厅

    张明杰教授是中国著名的结构生物学家，中国科学院院士、香港科学院创院院士，香港科技大学讲座教授，中国科学技术大学生命科学学院院长。1988年张明杰教授毕业于复旦大学；1993年获加拿大卡尔加里大学博士学位。1995年起受聘于香港科技大学生物化学系。现为香港科技大学嘉里理学教授，高等研究院高级研究员，分子神经科学国家重点实验室副主任。2004年起任深圳北京大学香港科技大学医学中心副主任，研究所所长。主要研究领域侧重于两个方向：支架蛋白构建神经信号传导复合体的生物化学和结构学基础；神经细胞极性产生及维持的机制研究。

   Synapses are semi-membraneless, protein-dense, sub-micron chemicalreaction compartments responsible for signal processing in each and everyneuron. Proper formation and dynamic responses to stimulations of synapses bothduring development and in adult are fundamental to functions of mammalianbrains. There are not any identical ones among trillions of synapses in a humanbrain. Using structural biology and biochemical reconstitution approaches, weshow that, both in solution and on supported membrane bilayers, multivalentinteraction networks formed by major excitatory postsynaptic density (PSD)scaffold proteins led to the formation of PSD-like assemblies via phaseseparation.A distinct feature of the phase transition-mediated assembly of PSDis that the molecular interactions are predominantly highly specific and highaffinity multi-valent protein-protein interactions instead of IDP-mediatedinteractions. The reconstituted PSD-like assemblies can cluster receptors,selectively concentrate enzymes, promote actin bundle formation, and expelinhibitory postsynaptic protein. Additionally, the condensed phase PSDassemblies have features that are distinct from those in homogeneous solutionsand fit for synaptic functions.Thus, a defined and biochemical trackablemolecular platform is reconstructed for understanding how neuronal synapses areformed and dynamically regulated.