Tyrosine phosphorylation of ionotropic glutamate receptors by Fyn or Src differentially modulates their susceptibility to calpain and enhances their binding to spectrin and PSD-95.
作者： Yongqi Rong , Xiaoying Lu , Anne Bernard , Michel Khrestchatisky , Michel Baudry
DOI: 10.1046/J.1471-4159.2001.00565.X
关键词: Tyrosine phosphorylation 、 SH2 domain 、 AMPA receptor 、 Receptor tyrosine kinase 、 Phosphorylation 、 Biochemistry 、 SRC Family Tyrosine Kinase 、 Proto-oncogene tyrosine-protein kinase Src 、 FYN 、 Cell biology 、 Biology
摘要: Both tyrosine phosphorylation and calpain-mediated truncation of ionotropic glutamate receptors are important mechanisms for synaptic plasticity. Previous work from our laboratory has shown that calpain activation results in the C-terminal domains several receptor subunits. To test whether how subunits modulates susceptibility, membranes were phosphorylated by Fyn or Src, two members Src family kinases. Tyrosine significantly reduced both NR2A NR2B NMDA receptors, but not GluR1 AMPA receptors. In contrast, with protected enhanced Similar observed domain fusion proteins before incubation calcium. addition, their binding to spectrin PSD-95. Thus, impairs facilitates subunits, depending on which kinase is activated. Such could serve regulate integrity location, addition modulating channel properties.
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