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首页> 外文期刊>Molecular and cellular neurosciences >Structure-function analysis of SAP97, a modular scaffolding protein that drives dendrite growth
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Structure-function analysis of SAP97, a modular scaffolding protein that drives dendrite growth

机译:SAP97的结构功能分析,SAP97是驱动树突生长的模块化脚手架蛋白

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摘要

Activation of AMPA receptors assembled with the GluA1 subunit can promote dendrite growth in a manner that depends on its direct binding partner, SAP97. SAP97 is a modular scaffolding protein that has at least seven recognizable protein protein interaction domains. Several complementary approaches were employed to show that the dendrite branching promoting action of full length SAP97 depends on ligand(s) that bind to the PDZ3 domain. Ligand(s) to PDZ1, PDZ2 and I3 domains also contribute to dendrite growth. The ability of PDZ3 ligand(s) to promote dendrite growth depends on localization at the plasma membrane along with GluA1 and SAP97. These results suggest that the assembly of a multi-protein complex at or near synapses is vital for the translation of AMPAR activity into dendrite growth. (C) 2015 Elsevier Inc. All rights reserved.
机译:组装有GluA1亚基的AMPA受体的激活可以以依赖于其直接结合伴侣SAP97的方式促进枝晶生长。 SAP97是一种模块化的支架蛋白,具有至少七个可识别的蛋白相互作用域。采用了几种互补的方法来显示全长SAP97的树枝状分支促进作用取决于与PDZ3域结合的配体。 PDZ1,PDZ2和I3域的配体也有助于枝晶生长。 PDZ3配体促进枝晶生长的能力取决于与GluA1和SAP97一起在质膜上的定位。这些结果表明在突触处或突触附近的多蛋白复合物的组装对于将AMPAR活性转化为树突生长至关重要。 (C)2015 Elsevier Inc.保留所有权利。

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