Department of Chemistry, Bielefeld University, Universitätsstrasse 25, 33615 Bielefeld, Germany.
Eur J Cell Biol. 2011 Nov;90(11):972-81. doi: 10.1016/j.ejcb.2010.11.014. Epub 2011 Jan 15.
The receptor tyrosine kinase Met plays a pivotal role in vertebrate development and tissue regeneration, its deregulation contributes to cancer. Met is also targeted during the infection by the facultative intracellular bacterium Listeria monocytogenes. The mechanistic basis for Met activation by its natural ligand hepatocyte growth factor/scatter factor (HGF/SF) is only beginning to be understood at a structural level. Crystal structures of Met in complex with L. monocytogenes InlB suggest that Met dimerization by this bacterial invasion protein is mediated by a dimer contact of the ligand. Here, I review the structural basis of Met activation by InlB and highlight parallels and differences to the physiological Met ligand HGF/SF and its splice variant NK1.
受体酪氨酸激酶 Met 在脊椎动物发育和组织再生中发挥着关键作用，其失调会导致癌症。在兼性细胞内细菌李斯特菌感染过程中，Met 也是靶向目标。Met 被其天然配体肝细胞生长因子/分散因子（HGF/SF）激活的机制基础仅在结构水平上开始被理解。Met 与李斯特菌 InlB 复合物的晶体结构表明，这种细菌入侵蛋白通过配体的二聚体接触介导 Met 二聚化。在这里，我回顾了 InlB 激活 Met 的结构基础，并强调了与生理 Met 配体 HGF/SF 及其剪接变体 NK1 的相似性和差异。
