Abstract

Pioneering bioinformatic analysis using sequence data revealed that teneurins evolved from bacterial tyrosine-aspartate (YD)-repeat protein precursors. Here, we discuss how structures of the C-terminal domain of teneurins, determined using X-ray crystallography and electron microscopy, support the earlier findings on the proteins’ ancestry. This chapter describes the structure of the teneurin scaffold with reference to a large family of teneurin-like proteins that are widespread in modern prokaryotes. The central scaffold of modern eukaryotic teneurins is decorated by additional domains typically found in bacteria, which are re-purposed in eukaryotes to generate highly multifunctional receptors. We discuss how alternative splicing contributed to further diversifying teneurin structure and thereby function. This chapter traces the evolution of teneurins from a structural point of view and presents the state-of-the-art of how teneurin function is encoded by its specific structural features.

Highlights

  • Teneurins are evolutionarily ancient cell surface receptors which have emerged as important regulators of many neurobiological processes in both vertebrates and invertebrates, including synaptic partner matching (Hong et al, 2012), synaptic organization (Mosca et al, 2012), neuronal migration (Drabikowski et al, 2005) and axonal guidance and targeting (Leamey et al, 2007; Berns et al, 2018)

  • This variety of functions has been attributed to both homophilic interactions between teneurins expressed on adjacent cells and heterophilic interactions with other cell surface receptors, such as the synaptic adhesion G-protein-coupled receptor, latrophilin, which is essential for hippocampal synapse formation in mice (Silva et al, 2011; Boucard et al, 2014; Anderson et al, 2017)

  • To avoid overlap with other chapters of this review series we focus our discussion on the structural features of teneurins with respect to their evolution from the bacterial protein ancestors

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Summary

Teneurin Structures Are Composed of Ancient Bacterial Protein Domains

Edited by: Antony Jr. Boucard, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional (CINVESTAV), Mexico. Specialty section: This article was submitted to Neuroendocrine Science, a section of the journal

Frontiers in Neuroscience
INTRODUCTION
THE TENEURIN SCAFFOLD
TENEURIN DOMAINS DOWNSTREAM OF THE SCAFFOLD
CONCLUDING REMARKS
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