Abstract
Teneurins belong to a family of synaptic adhesion molecules widely expressed in the nervous system. These transmembrane proteins form cis-dimers and data suggest they interact across the synapse either homo- or heterophilically. Our previous research has shown that individual teneurins are responsible for the establishment of functionally distinct neural circuits. However, the molecular basis how to mediate synaptic specificity is unknown. Although there are predictions regarding the protein domains for cis- and trans-interactions, no detailed protein structure has yet been solved. This project aims at identifying the molecular teneurin structure to model their protein interactions and thus explain biological functionality.
References
- Mosca, T. J. (2015) On the Teneurin track: a new synaptic organization molecule emerges. Front Cell Neurosci 9, 204.
- Antinucci, P., Suleyman, O., Monfries, C. & Hindges, R. (2016) Neural Mechanisms Generating Orientation Selectivity in the Retina. Curr Biol 26, 1802-1815
- Seiradake E, del Toro D, Nagel D, Cop F, Härtl R, Ruff T, Seyit-Bremer G, Harlos K, Border EC, Acker-Palmer A, Jones EY, Klein R. (2014). FLRT structure: balancing repulsion and cell adhesion in cortical and vascular development. Neuron 84:370-385.
- De Nicola GF, Martin ED, Chaikuad A, Bassi R, Clark J, Martino L, Verma S, Sicard P, Tata R, Atkinson RA, Knapp S, Conte MR, Marber MS. (2013). Mechanism and consequence of the autoactivation of p38α mitogen-activated protein kinase promoted by TAB1. Nat Struct Mol Biol. 20:1182-1190.