亲缘关系
外域
相互作用体
神经元
结合亲和力
神经科学
生物
细胞生物学
化学
生物化学
受体
基因
作者
Filip Cosmanescu,Phinikoula S. Katsamba,Alina P. Sergeeva,Göran Ahlsén,Sunny Patel,Joshua Brewer,Liming Tan,Shansheng Xu,Qi Xiao,Sonal Nagarkar-Jaiswal,Aljoscha Nern,Hugo J. Bellen,S. Lawrence Zipursky,Barry Honig,Lawrence Shapiro
出处
期刊:Neuron
[Elsevier]
日期:2018-12-01
卷期号:100 (6): 1385-1400.e6
被引量:64
标识
DOI:10.1016/j.neuron.2018.10.046
摘要
Summary
Binding between DIP and Dpr neuronal recognition proteins has been proposed to regulate synaptic connections between lamina and medulla neurons in the Drosophila visual system. Each lamina neuron was previously shown to express many Dprs. Here, we demonstrate, by contrast, that their synaptic partners typically express one or two DIPs, with binding specificities matched to the lamina neuron-expressed Dprs. A deeper understanding of the molecular logic of DIP/Dpr interaction requires quantitative studies on the properties of these proteins. We thus generated a quantitative affinity-based DIP/Dpr interactome for all DIP/Dpr protein family members. This revealed a broad range of affinities and identified homophilic binding for some DIPs and some Dprs. These data, along with full-length ectodomain DIP/Dpr and DIP/DIP crystal structures, led to the identification of molecular determinants of DIP/Dpr specificity. This structural knowledge, along with a comprehensive set of quantitative binding affinities, provides new tools for functional studies in vivo.
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