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Instruments / Technical Area	Publication Details	Published	Actions
B21-High Throughput SAXS	Teneurin4 dimer structures reveal a calcium‐stabilized compact conformation supporting homomeric trans‐interactions Dimphna H Meijer , Cátia P Frias , J. Wouter Beugelink , Yanthi N. Deurloo , Bert J. C. Janssen The Embo Journal 66 DOI: 10.15252/embj.2020107505 Diamond Proposal Number(s): [19800] Open Access Show Abstract ▼ Abstract: Establishment of correct synaptic connections is a crucial step during neural circuitry formation. The Teneurin family of neuronal transmembrane proteins promotes cell–cell adhesion via homophilic and heterophilic interactions, and is required for synaptic partner matching in the visual and hippocampal systems in vertebrates. It remains unclear how individual Teneurins form macromolecular cis- and trans-synaptic protein complexes. Here, we present a 2.7 Å cryo-EM structure of the dimeric ectodomain of human Teneurin4. The structure reveals a compact conformation of the dimer, stabilized by interactions mediated by the C-rich, YD-shell, and ABD domains. A 1.5 Å crystal structure of the C-rich domain shows three conserved calcium binding sites, and thermal unfolding assays and SAXS-based rigid-body modeling demonstrate that the compactness and stability of Teneurin4 dimers are calcium-dependent. Teneurin4 dimers form a more extended conformation in conditions that lack calcium. Cellular assays reveal that the compact cis-dimer is compatible with homomeric trans-interactions. Together, these findings support a role for teneurins as a scaffold for macromolecular complex assembly and the establishment of cis- and trans-synaptic interactions to construct functional neuronal circuits.	Jan 2022
I03-Macromolecular Crystallography	Structures of Teneurin adhesion receptors reveal an ancient fold for cell-cell interaction Verity A. Jackson , Dimphna H. Meijer , Maria Carrasquero , Laura S. Van Bezouwen , Edward D. Lowe , Colin Kleanthous , Bert J. C. Janssen , Elena Seiradake Nature Communications 9 DOI: 10.1038/s41467-018-03460-0 Diamond Proposal Number(s): [12346, 1838] Open Access Show 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.	Mar 2018

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