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

Autor: Jackson, Verity A, Meijer, Dimphna H, Carrasquero, Maria, van Bezouwen, Laura S, Lowe, Edward D, Kleanthous, Colin, Janssen, Bert J C, Seiradake, Elena, Crystal and Structural Chemistry, Sub Crystal and Structural Chemistry, Sub Cryo - EM, Cryo-EM
Jazyk: angličtina
Rok vydání: 2018
Předmět:
Zdroj: Nature Communications, 9(1). Nature Publishing Group
ISSN: 2041-1723
Popis: 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.
Databáze: OpenAIRE