Slitrk2-PTPδ复合物的结构揭示了剪接依赖性反式突触粘附的机制。
Structure of Slitrk2-PTPδ complex reveals mechanisms for splicing-dependent trans-synaptic adhesion.
作者信息
Yamagata Atsushi, Sato Yusuke, Goto-Ito Sakurako, Uemura Takeshi, Maeda Asami, Shiroshima Tomoko, Yoshida Tomoyuki, Fukai Shuya
机构信息
1] Structural Biology Laboratory, Life Science Division, Synchrotron Radiation Research Organization and Institute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo 113-0032, Japan [2] Department of Medical Genome Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Chiba 277-8501, Japan [3] CREST, JST, Saitama 332-0012, Japan.
1] Structural Biology Laboratory, Life Science Division, Synchrotron Radiation Research Organization and Institute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo 113-0032, Japan [2] CREST, JST, Saitama 332-0012, Japan.
出版信息
Sci Rep. 2015 May 19;5:9686. doi: 10.1038/srep09686.
Selective binding between pre- and postsynaptic adhesion molecules can induce synaptic differentiation. Here we report the crystal structure of a synaptogenic trans-synaptic adhesion complex between Slit and Trk-like family member 2 (Slitrk2) and receptor protein tyrosine phosphatase (RPTP) δ. The structure and site-directed mutational analysis revealed the structural basis of splicing-dependent adhesion between Slitrks and type IIa RPTPs for inducing synaptic differentiation.
突触前和突触后黏附分子之间的选择性结合可诱导突触分化。在此，我们报告了Slit与类Trk家族成员2（Slitrk2）和受体蛋白酪氨酸磷酸酶（RPTP）δ之间的一种促突触形成的跨突触黏附复合物的晶体结构。该结构及定点突变分析揭示了Slitrks与IIa型RPTPs之间剪接依赖性黏附以诱导突触分化的结构基础。
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