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Cell Rep 2020 Feb 25;308:2655-2671.e7. doi: 10.1016/j.celrep.2020.02.003.
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Family-wide Structural and Biophysical Analysis of Binding Interactions among Non-clustered δ-Protocadherins.

Harrison OJ , Brasch J , Katsamba PS , Ahlsen G , Noble AJ , Dan H , Sampogna RV , Potter CS , Carragher B , Honig B , Shapiro L .

Non-clustered δ1- and δ2-protocadherins, close relatives of clustered protocadherins, function in cell adhesion and motility and play essential roles in neural patterning. To understand the molecular interactions underlying these functions, we used solution biophysics to characterize binding of δ1- and δ2-protocadherins, determined crystal structures of ectodomain complexes from each family, and assessed ectodomain assembly in reconstituted intermembrane junctions by cryoelectron tomography (cryo-ET). Homophilic trans (cell-cell) interactions were preferred for all δ-protocadherins, with additional weaker heterophilic interactions observed exclusively within each subfamily. As expected, δ1- and δ2-protocadherin trans dimers formed through antiparallel EC1-EC4 interfaces, like clustered protocadherins. However, no ectodomain-mediated cis (same-cell) interactions were detectable in solution; consistent with this, cryo-ET of reconstituted junctions revealed dense assemblies lacking the characteristic order observed for clustered protocadherins. Our results define non-clustered protocadherin binding properties and their structural basis, providing a foundation for interpreting their functional roles in neural patterning.

PubMed ID: 32101743
Article link: Cell Rep
Grant support: [+]

Genes referenced: pcdh1 pcdh10 pcdh12 pcdh17 pcdh18 pcdh19 pcdh7 pcdh8 pcdh8.2 pcdh9 spr
GO keywords: cell adhesion [+]

Article Images: [+] show captions
References [+] :
Adams, PHENIX: a comprehensive Python-based system for macromolecular structure solution. 2010, Pubmed