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

DOI: 10.1038/s41467-018-03460-0 DOI Help

Authors: Verity A. Jackson (Oxford University) , Dimphna H. Meijer (Utrecht University) , Maria Carrasquero (Oxford University) , Laura S. Van Bezouwen (Utrecht University) , Edward D. Lowe (Oxford University) , Colin Kleanthous (Oxford University) , Bert J. C. Janssen (Utrecht University) , Elena Seiradake (Oxford University)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 9

State: Published (Approved)
Published: March 2018
Diamond Proposal Number(s): 12346 , 1838

Open Access Open Access

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.

Journal Keywords: Bacterial toxins; Development of the nervous system; Electron microscopy; X-ray crystallography

Subject Areas: Biology and Bio-materials, Chemistry

Instruments: I03-Macromolecular Crystallography

Other Facilities: ESRF