Neuron-Subtype-Specific Expression, Interaction Affinities, and Specificity Determinants of DIP/Dpr Cell Recognition Proteins.
Neuron-Subtype-Specific Expression, Interaction Affinities, and Specificity Determinants of DIP/Dpr Cell Recognition Proteins.
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DIP/Dpr 细胞识别蛋白的神经元亚型特异性表达、相互作用亲和力和特异性决定因素。
DOI:
10.1016/j.neuron.2018.10.046
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发表时间:
2018-12-19
期刊:
影响因子:
16.2
通讯作者:
Shapiro L
中科院分区:
文献类型:
--
作者:
Cosmanescu F;Katsamba PS;Sergeeva AP;Ahlsen G;Patel SD;Brewer JJ;Tan L;Xu S;Xiao Q;Nagarkar-Jaiswal S;Nern A;Bellen HJ;Zipursky SL;Honig B;Shapiro L
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. DIP/Dpr interactions help to pattern the Drosophila nervous system. Cosmanescu et al. quantify their interactions and map DIP expression in medulla neurons. Structural studies identify specificity determinants of DIP/Dpr interactions and reveal a conserved architecture for DIP/DIP homodimers.
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DOI:
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发表时间:
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期刊:
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影响因子:
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DOI:
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发表时间:
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期刊:
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影响因子:
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