高尔基体堆叠蛋白GRASP65和卵泡抑素样蛋白Fstl1的结构研究
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摘要
高尔基体在蛋白质和脂类的加工、修饰、分选、运输等许多方面起着至关重要的作用。哺乳动物高尔基体的扁平囊堆叠之间依靠管状结构侧向连接形成了高尔基体带状结构。高尔基体堆叠蛋白GRASP65(Golgi ReAssembly Stacking Protein, GRASP65)位于高尔基体顺面及顺面网。作为维系高尔基体的支架蛋白,GRASP65在与其它蛋白的共同作用下参与高尔基体顺面的侧向连接。
磷酸化GRASP65会使GRASP65反式寡聚体解聚,引起高尔基体的去堆叠和片段化。高尔基体的片段化对于细胞周期进程和生长分裂至关重要。此外,GRASP65在纺锤体形成、细胞凋亡、非常规的蛋白运输等方面发挥重要作用。
本文首次解析了GRASP65GRASP结构域的三维晶体结构。基于结构,比较和分析了该结构域与同源蛋白之间的结构异同。在体外生化试验中进行了一系列的点突变,初步确定了引起蛋白聚合的关键氨基酸位点,并对这些位点导致聚集状态变化的可能原因进行了分析和阐述。随后,对这些突变体进行了细胞内的功能实验,进一步验证了这些位点对高尔基体堆叠的影响。本论文对GRASP65GRASP结构域的解析,为理解高尔基体顺面堆叠蛋白的作用机制奠定了结构学基础。
此外,利用果蝇S2表达系统获得了分泌型糖蛋白Follistatin-likel(Fstl1). Fstl1在肺部发育、输尿管发育以及骨骼发育等许多发育过程中都发挥着重要的调控作用。首次解析得到了Fstl1蛋白N-端FOLN-KAZAL结构域的三维晶体结构,分析了Fstl1的FOLN-KAZAL结构域与其它含有KAZAL结构域的蛋白在序列和折叠方式上的显著差异。Fstl1与其同源蛋白在配体结合及功能等方面存在差异,本论文对Fstll FOLN-KAZAL结构域的解析,为了解和分析Fstl1与其同源蛋白在配体结合和功能上的差异提供了结构上的依据,也为Fstl1参与调控的疾病的预防和治疗提供了线索。
The Golgi apparatus play crucial roles in processing and glycosylation of proteins and lipids. It is also responsible for protein sorting and transportation. In mammalian cells, the Golgi apparatus consists of many stacks of cisternae, which are laternally linked by tubules forming the Golgi ribbon.The GRASP65(Golgi ReAssembly Stacking Protein65) is found at cis-golgi and cis-golgi network. As a scaffold protein, GRASP65together with other proteins, participates in laternally linking of stacks.
GRASP65phosphorylation leads to trans-oligomer disassembly, and eventurally results in Golgi ribbon unlinking and fragmentation. The fragmentation of Golgi apparatus is crucial for cell-cycle and mitosis progression. In addition, The Golgi apparatus is involved in the formation of spindle, apoptosis and unconventional secretion in the cell.
The crystal structure of GRASP65GRASP domain was determined. It is the first high resolution structure reported for GRASP65. The difference between GRASP65and its homologous proteins were analyzed based on their crystal structures. Critical residues involved in protein polymerization were identified, and roles of these residues on dimerization and oligomerization were analyzed by series of mutations. To verify the significance of these mutations, the mutant proteins were overexpressed within the Hela cell, and their effect on Golgi stacking were checked by confocal microscopy. Overall, from molecular structure to cell level, our research provides a basis for understanding the stacking mechanism of this cis-golgi stacking protein.
Moreover, the secretory glycoprotein follistatin-likel (Fstl1) have been successfully expressed in Drosophila S2cell. Fstll play important roles in mediating many developmental processes, such as lung development, ureter development and skeleton development. Different ligand binding and function exist between Fstll and its homologous proteins. The crystal structure of Fstll FOLN-KAZAL domain was determined. The difference between Fstll FOLN-KAZAL domain and that of homologous proteins were compared. The crystal structure of Fstll FOLN-KAZAL domain is helpful in illustrating the different function of these proteins, and may provide clues for the prevention and treatment of Fstll-related diseases.
磷酸化GRASP65会使GRASP65反式寡聚体解聚,引起高尔基体的去堆叠和片段化。高尔基体的片段化对于细胞周期进程和生长分裂至关重要。此外,GRASP65在纺锤体形成、细胞凋亡、非常规的蛋白运输等方面发挥重要作用。
本文首次解析了GRASP65GRASP结构域的三维晶体结构。基于结构,比较和分析了该结构域与同源蛋白之间的结构异同。在体外生化试验中进行了一系列的点突变,初步确定了引起蛋白聚合的关键氨基酸位点,并对这些位点导致聚集状态变化的可能原因进行了分析和阐述。随后,对这些突变体进行了细胞内的功能实验,进一步验证了这些位点对高尔基体堆叠的影响。本论文对GRASP65GRASP结构域的解析,为理解高尔基体顺面堆叠蛋白的作用机制奠定了结构学基础。
此外,利用果蝇S2表达系统获得了分泌型糖蛋白Follistatin-likel(Fstl1). Fstl1在肺部发育、输尿管发育以及骨骼发育等许多发育过程中都发挥着重要的调控作用。首次解析得到了Fstl1蛋白N-端FOLN-KAZAL结构域的三维晶体结构,分析了Fstl1的FOLN-KAZAL结构域与其它含有KAZAL结构域的蛋白在序列和折叠方式上的显著差异。Fstl1与其同源蛋白在配体结合及功能等方面存在差异,本论文对Fstll FOLN-KAZAL结构域的解析,为了解和分析Fstl1与其同源蛋白在配体结合和功能上的差异提供了结构上的依据,也为Fstl1参与调控的疾病的预防和治疗提供了线索。
The Golgi apparatus play crucial roles in processing and glycosylation of proteins and lipids. It is also responsible for protein sorting and transportation. In mammalian cells, the Golgi apparatus consists of many stacks of cisternae, which are laternally linked by tubules forming the Golgi ribbon.The GRASP65(Golgi ReAssembly Stacking Protein65) is found at cis-golgi and cis-golgi network. As a scaffold protein, GRASP65together with other proteins, participates in laternally linking of stacks.
GRASP65phosphorylation leads to trans-oligomer disassembly, and eventurally results in Golgi ribbon unlinking and fragmentation. The fragmentation of Golgi apparatus is crucial for cell-cycle and mitosis progression. In addition, The Golgi apparatus is involved in the formation of spindle, apoptosis and unconventional secretion in the cell.
The crystal structure of GRASP65GRASP domain was determined. It is the first high resolution structure reported for GRASP65. The difference between GRASP65and its homologous proteins were analyzed based on their crystal structures. Critical residues involved in protein polymerization were identified, and roles of these residues on dimerization and oligomerization were analyzed by series of mutations. To verify the significance of these mutations, the mutant proteins were overexpressed within the Hela cell, and their effect on Golgi stacking were checked by confocal microscopy. Overall, from molecular structure to cell level, our research provides a basis for understanding the stacking mechanism of this cis-golgi stacking protein.
Moreover, the secretory glycoprotein follistatin-likel (Fstl1) have been successfully expressed in Drosophila S2cell. Fstll play important roles in mediating many developmental processes, such as lung development, ureter development and skeleton development. Different ligand binding and function exist between Fstll and its homologous proteins. The crystal structure of Fstll FOLN-KAZAL domain was determined. The difference between Fstll FOLN-KAZAL domain and that of homologous proteins were compared. The crystal structure of Fstll FOLN-KAZAL domain is helpful in illustrating the different function of these proteins, and may provide clues for the prevention and treatment of Fstll-related diseases.
引文
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[9]Nakamura N., Emerging new roles of gm 130, a cis-golgi matrix protein,in higher order cell functions. J Pharmacol Sci,2010.112(3):255-264.
[10]Marra P., Salvatore L., Mironov A., et al. The biogenesis of the golgi ribbon:The roles of membrane input from the er and of gm130. Mol Biol Cell,2007.18 (5):1595-1608.
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