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首页> 外文期刊>Neuron >Calcium-permeable AMPA receptor plasticity is mediated by subunit-specific interactions with PICK1 and NSF.
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Calcium-permeable AMPA receptor plasticity is mediated by subunit-specific interactions with PICK1 and NSF.

机译：钙可渗透的AMPA受体可塑性由与PICK1和NSF的亚基特异性相互作用介导。

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摘要

A recently described form of synaptic plasticity results in dynamic changes in the calcium permeability of synaptic AMPA receptors. Since the AMPA receptor GluR2 subunit confers calcium permeability, this plasticity is thought to occur through the dynamic exchange of synaptic GluR2-lacking and GluR2-containing receptors. To investigate the molecular mechanisms underlying this calcium-permeable AMPA receptor plasticity (CARP), we examined whether AMPA receptor exchange was mediated by subunit-specific protein-protein interactions. We found that two GluR2-interacting proteins, the PDZ domain-containing Protein interacting with C kinase (PICK1) and N-ethylmaleimide sensitive fusion protein (NSF), are specifically required for CARP. Furthermore, PICK1, but not NSF, regulates the formation of extrasynaptic plasma membrane pools of GluR2-containing receptors that may be laterally mobilized into synapses during CARP. These results demonstrate that PICK1 and NSF dynamically regulate the synaptic delivery of GluR2-containing receptors during CARP and thus regulate the calcium permeability of AMPA receptors at excitatory synapses.
机译：最近描述的一种形式的突触可塑性导致突触AMPA受体的钙渗透性动态变化。由于AMPA受体GluR2亚基赋予钙渗透性，这种可塑性被认为是通过动态交换缺乏突触GluR2和含有GluR2的受体而发生的。为了研究这种钙可渗透的AMPA受体可塑性（CARP）的分子机制，我们检查了AMPA受体的交换是否由亚基特异性蛋白-蛋白相互作用介导。我们发现CARP特别需要两个与GluR2相互作用的蛋白质，即与C激酶（PICK1）和N-乙基马来酰亚胺敏感的融合蛋白（NSF）相互作用的含PDZ域的蛋白质。此外，PICK1（而不是NSF）调节含有GluR2的受体的突触外质膜池的形成，该受体在CARP期间可横向移动到突触中。这些结果表明，PICK1和NSF在CARP期间动态调节含GluR2受体的突触传递，从而调节兴奋性突触处AMPA受体的钙渗透性。

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