Structural Basis of Diverse Homophilic Recognition by Clustered α- and β-Protocadherins

Goodman, Kerry  Marie; Rubinstein, Rotem; Thu, Chan  Aye; Bahna, Fabiana; Mannepalli, Seetha; Ahlsén, Göran; Rittenhouse, Chelsea; Maniatis, Tom; Honig, Barry; Shapiro, Lawrence

doi:10.1016/j.neuron.2016.04.004

Title: Structural Basis of Diverse Homophilic Recognition by Clustered α- and β-Protocadherins

Journal Article · Thu May 05 00:00:00 EDT 2016 · Neuron

DOI:https://doi.org/10.1016/j.neuron.2016.04.004· OSTI ID:1255307

Goodman, Kerry Marie ^[1]; Rubinstein, Rotem ^[1]; Thu, Chan Aye ^[1]; Bahna, Fabiana ^[1]; Mannepalli, Seetha ^[1]; Ahlsén, Göran ^[1]; Rittenhouse, Chelsea ^[1]; Maniatis, Tom ^[1]; Honig, Barry ^[1]; Shapiro, Lawrence ^[1]

Columbia Univ., New York, NY (United States)

Clustered protocadherin proteins (α-, β-, and γ-Pcdhs) provide a high level of cell-surface diversity to individual vertebrate neurons, engaging in highly specific homophilic interactions to mediate important roles in mammalian neural circuit development. How Pcdhs bind homophilically through their extracellular cadherin (EC) domains among dozens of highly similar isoforms has not been determined. Here, we report crystal structures for extracellular regions from four mouse Pcdh isoforms (α4, α7, β6, and β8), revealing a canonical head-to-tail interaction mode for homophilic trans dimers comprising primary intermolecular EC1:EC4 and EC2:EC3 interactions. A subset of trans interface residues exhibit isoform-specific conservation, suggesting roles in recognition specificity. Mutation of these residues, along with trans-interacting partner residues, altered the specificities of Pcdh interactions. Altogether, these data show how sequence variation among Pcdh isoforms encodes their diverse strict homophilic recognition specificities, which are required for their key roles in neural circuit assembly.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: National Institutes of Health (NIH); National Science Foundation (NSF)

Grant/Contract Number:: P41 GM103403; MCB-1412472; R01GM062270; R01GM107571

OSTI ID:: 1255307

Journal Information:: Neuron, Vol. 90, Issue 4; ISSN 0896-6273

Publisher:: Cell Press - ElsevierCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 57 works

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