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Goodman, Kerry M. ; Rubinstein, Rotem ; Dan, Hanbin ; Bahna, Fabiana ; Mannepalli, Seetha ; Ahlsén, Göran ; Aye Thu, Chan ; Sampogna, Rosemary V. ; Maniatis, Tom ; Honig, Barry ; et al ( , Proceedings of the National Academy of Sciences)
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Larsen, Ida Signe ; Narimatsu, Yoshiki ; Joshi, Hiren Jitendra ; Siukstaite, Lina ; Harrison, Oliver J. ; Brasch, Julia ; Goodman, Kerry M. ; Hansen, Lars ; Shapiro, Lawrence ; Honig, Barry ; et al ( , Proceedings of the National Academy of Sciences)
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Goodman, Kerry M ; Yamagata, Masahito ; Jin, Xiangshu ; Mannepalli, Seetha ; Katsamba, Phinikoula S ; Ahlsén, Göran ; Sergeeva, Alina P ; Honig, Barry ; Sanes, Joshua R ; Shapiro, Lawrence ( , eLife)Sidekick (Sdk) 1 and 2 are related immunoglobulin superfamily cell adhesion proteins required for appropriate synaptic connections between specific subtypes of retinal neurons. Sdks mediate cell-cell adhesion with homophilic specificity that underlies their neuronal targeting function. Here we report crystal structures of Sdk1 and Sdk2 ectodomain regions, revealing similar homodimers mediated by the four N-terminal immunoglobulin domains (Ig1–4), arranged in a horseshoe conformation. These Ig1–4 horseshoes interact in a novel back-to-back orientation in both homodimers through Ig1:Ig2, Ig1:Ig1 and Ig3:Ig4 interactions. Structure-guided mutagenesis results show that this canonical dimer is required for both Sdk-mediated cell aggregation (via trans interactions) and Sdk clustering in isolated cells (via cis interactions). Sdk1/Sdk2 recognition specificity is encoded across Ig1–4, with Ig1–2 conferring the majority of binding affinity and differential specificity. We suggest that competition between cis and trans interactions provides a novel mechanism to sharpen the specificity of cell-cell interactions.more » « less