Abstract：
: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.
journal_name
Neuronjournal_title
Neuronauthors
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 Ldoi
10.1016/j.neuron.2018.10.046subject
Has Abstractpub_date
2018-12-19 00:00:00pages
1385-1400.e6issue
6eissn
0896-6273issn
1097-4199pii
S0896-6273(18)30954-1journal_volume
100pub_type
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