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  Structural Basis of Latrophilin-FLRT Interaction

Jackson, V. A., del Toro, D., Carrasquero, M., Roversi, P., Harlos, K., Klein, R., et al. (2015). Structural Basis of Latrophilin-FLRT Interaction. STRUCTURE, 23(4), 774-781. doi:10.1016/j.str.2015.01.013.

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 Creators:
Jackson, Verity A.1, Author
del Toro, Daniel2, Author              
Carrasquero, Maria1, Author
Roversi, Pietro1, Author
Harlos, Karl1, Author
Klein, Rüdiger2, Author              
Seiradake, Elena1, Author
Affiliations:
1external, ou_persistent22              
2Department: Molecules-Signaling-Development / Klein, MPI of Neurobiology, Max Planck Society, ou_1113546              

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Free keywords: ALPHA-LATROTOXIN RECEPTOR; CELL-ADHESION; OLFACTOMEDIN DOMAIN; GLUTAMINYL CYCLASE; BINDING PROTEIN; ADHD; GENE; SUSCEPTIBILITY; IDENTIFICATION; CONSERVATION
 Abstract: Latrophilins, receptors for spider venom alpha-latrotoxin, are adhesion type G-protein-coupled receptors with emerging functions in synapse development. The N-terminal region binds the endogenous cell adhesion molecule FLRT, a major regulator of cortical and synapse development. We present crystallographic data for the mouse Latrophilin3 lectin and olfactomedin-like (Olf) domains, thereby revealing the Olf beta-propeller fold and conserved calcium-binding site. We locate the FLRT-Latrophilin binding surfaces by a combination of sequence conservation analysis, point mutagenesis, and surface plasmon resonance experiments. In stripe assays, we show that wild-type Latrophilin3 and its high-affinity interactor FLRT2, but not the binding-impaired mutants we generated, promote HeLa cell adhesion. In contrast, cortical neurons expressing endogenous FLRTs are repelled by wild-type Latrophilin3 and not by the binding-impaired mutant. Taken together, we present molecular level insights into Latrophilin structure, its FLRT-binding mechanism, and a role for Latrophilin and FLRT that goes beyond a simply adhesive interaction.

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Language(s): eng - English
 Dates: 2015
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000352507400020
DOI: 10.1016/j.str.2015.01.013
 Degree: -

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Title: STRUCTURE
Source Genre: Journal
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Publ. Info: 600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA : CELL PRESS
Pages: - Volume / Issue: 23 (4) Sequence Number: - Start / End Page: 774 - 781 Identifier: ISSN: 0969-2126