Super-complexes of adhesion GPCRs and neural guidance receptors

FLRT proteins are known to interact with Lphns and Unc5s, mediating cell adhesion and repulsion respectively. Here the authors use crystallography, native mass spectrometry, molecular dynamics simulations and cell-based assays to show that these three proteins form large super-complexes with functio...

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Autores principales: Verity A. Jackson, Shahid Mehmood, Matthieu Chavent, Pietro Roversi, Maria Carrasquero, Daniel del Toro, Goenuel Seyit-Bremer, Fanomezana M. Ranaivoson, Davide Comoletti, Mark S. P. Sansom, Carol V. Robinson, Rüdiger Klein, Elena Seiradake
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Lenguaje:EN
Publicado: Nature Portfolio 2016
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Acceso en línea:https://doaj.org/article/ef384409442e4b9a8531b5fb0fc42da1
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spelling oai:doaj.org-article:ef384409442e4b9a8531b5fb0fc42da12021-12-02T16:49:41ZSuper-complexes of adhesion GPCRs and neural guidance receptors10.1038/ncomms111842041-1723https://doaj.org/article/ef384409442e4b9a8531b5fb0fc42da12016-04-01T00:00:00Zhttps://doi.org/10.1038/ncomms11184https://doaj.org/toc/2041-1723FLRT proteins are known to interact with Lphns and Unc5s, mediating cell adhesion and repulsion respectively. Here the authors use crystallography, native mass spectrometry, molecular dynamics simulations and cell-based assays to show that these three proteins form large super-complexes with functions distinct from their smaller subcomplexes.Verity A. JacksonShahid MehmoodMatthieu ChaventPietro RoversiMaria CarrasqueroDaniel del ToroGoenuel Seyit-BremerFanomezana M. RanaivosonDavide ComolettiMark S. P. SansomCarol V. RobinsonRüdiger KleinElena SeiradakeNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-13 (2016)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Verity A. Jackson
Shahid Mehmood
Matthieu Chavent
Pietro Roversi
Maria Carrasquero
Daniel del Toro
Goenuel Seyit-Bremer
Fanomezana M. Ranaivoson
Davide Comoletti
Mark S. P. Sansom
Carol V. Robinson
Rüdiger Klein
Elena Seiradake
Super-complexes of adhesion GPCRs and neural guidance receptors
description FLRT proteins are known to interact with Lphns and Unc5s, mediating cell adhesion and repulsion respectively. Here the authors use crystallography, native mass spectrometry, molecular dynamics simulations and cell-based assays to show that these three proteins form large super-complexes with functions distinct from their smaller subcomplexes.
format article
author Verity A. Jackson
Shahid Mehmood
Matthieu Chavent
Pietro Roversi
Maria Carrasquero
Daniel del Toro
Goenuel Seyit-Bremer
Fanomezana M. Ranaivoson
Davide Comoletti
Mark S. P. Sansom
Carol V. Robinson
Rüdiger Klein
Elena Seiradake
author_facet Verity A. Jackson
Shahid Mehmood
Matthieu Chavent
Pietro Roversi
Maria Carrasquero
Daniel del Toro
Goenuel Seyit-Bremer
Fanomezana M. Ranaivoson
Davide Comoletti
Mark S. P. Sansom
Carol V. Robinson
Rüdiger Klein
Elena Seiradake
author_sort Verity A. Jackson
title Super-complexes of adhesion GPCRs and neural guidance receptors
title_short Super-complexes of adhesion GPCRs and neural guidance receptors
title_full Super-complexes of adhesion GPCRs and neural guidance receptors
title_fullStr Super-complexes of adhesion GPCRs and neural guidance receptors
title_full_unstemmed Super-complexes of adhesion GPCRs and neural guidance receptors
title_sort super-complexes of adhesion gpcrs and neural guidance receptors
publisher Nature Portfolio
publishDate 2016
url https://doaj.org/article/ef384409442e4b9a8531b5fb0fc42da1
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