Structures of Teneurin adhesion receptors reveal an ancient fold for cell-cell interaction

Verity A. Jackson (), Dimphna H. Meijer, Maria Carrasquero, Laura S. Bezouwen, Edward D. Lowe, Colin Kleanthous, Bert J. C. Janssen and Elena Seiradake ()
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Verity A. Jackson: Oxford University
Dimphna H. Meijer: Utrecht University
Maria Carrasquero: Oxford University
Laura S. Bezouwen: Utrecht University
Edward D. Lowe: Oxford University
Colin Kleanthous: Oxford University
Bert J. C. Janssen: Utrecht University
Elena Seiradake: Oxford University

Nature Communications, 2018, vol. 9, issue 1, 1-9

Abstract: Abstract Teneurins are ancient cell–cell adhesion receptors that are vital for brain development and synapse organisation. They originated in early metazoan evolution through a horizontal gene transfer event when a bacterial YD-repeat toxin fused to a eukaryotic receptor. We present X-ray crystallography and cryo-EM structures of two Teneurins, revealing a ~200 kDa extracellular super-fold in which eight sub-domains form an intricate structure centred on a spiralling YD-repeat shell. An alternatively spliced loop, which is implicated in homophilic Teneurin interaction and specificity, is exposed and thus poised for interaction. The N-terminal side of the shell is ‘plugged’ via a fibronectin-plug domain combination, which defines a new class of YD proteins. Unexpectedly, we find that these proteins are widespread amongst modern bacteria, suggesting early metazoan receptor evolution from a distinct class of proteins, which today includes both bacterial proteins and eukaryotic Teneurins.

Date: 2018
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DOI: 10.1038/s41467-018-03460-0

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