Frizzled 7 and PIP2 binding by syntenin PDZ2 domain supports Frizzled 7 trafficking and signalling

PDZ domain-containing proteins are known to function as intracellular scaffolds. Here, Egea-Jimenez et al. report the structure of the tandem PDZ domains of syntenin in complex with a Frizzled 7 peptide and PIP2, show that the ligands bind to syntenin cooperatively and illustrate the role of the com...

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Autores principales:	Antonio Luis Egea-Jimenez, Rodrigo Gallardo, Abel Garcia-Pino, Ylva Ivarsson, Anna Maria Wawrzyniak, Rudra Kashyap, Remy Loris, Joost Schymkowitz, Frederic Rousseau, Pascale Zimmermann
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/6a135f7cced44db1b5f72b08dd72540d
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spelling	oai:doaj.org-article:6a135f7cced44db1b5f72b08dd72540d2021-12-02T14:40:11ZFrizzled 7 and PIP2 binding by syntenin PDZ2 domain supports Frizzled 7 trafficking and signalling10.1038/ncomms121012041-1723https://doaj.org/article/6a135f7cced44db1b5f72b08dd72540d2016-07-01T00:00:00Zhttps://doi.org/10.1038/ncomms12101https://doaj.org/toc/2041-1723PDZ domain-containing proteins are known to function as intracellular scaffolds. Here, Egea-Jimenez et al. report the structure of the tandem PDZ domains of syntenin in complex with a Frizzled 7 peptide and PIP2, show that the ligands bind to syntenin cooperatively and illustrate the role of the complex for Frizzled 7 function.Antonio Luis Egea-JimenezRodrigo GallardoAbel Garcia-PinoYlva IvarssonAnna Maria WawrzyniakRudra KashyapRemy LorisJoost SchymkowitzFrederic RousseauPascale ZimmermannNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-13 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Antonio Luis Egea-Jimenez Rodrigo Gallardo Abel Garcia-Pino Ylva Ivarsson Anna Maria Wawrzyniak Rudra Kashyap Remy Loris Joost Schymkowitz Frederic Rousseau Pascale Zimmermann Frizzled 7 and PIP2 binding by syntenin PDZ2 domain supports Frizzled 7 trafficking and signalling
description	PDZ domain-containing proteins are known to function as intracellular scaffolds. Here, Egea-Jimenez et al. report the structure of the tandem PDZ domains of syntenin in complex with a Frizzled 7 peptide and PIP2, show that the ligands bind to syntenin cooperatively and illustrate the role of the complex for Frizzled 7 function.
format	article
author	Antonio Luis Egea-Jimenez Rodrigo Gallardo Abel Garcia-Pino Ylva Ivarsson Anna Maria Wawrzyniak Rudra Kashyap Remy Loris Joost Schymkowitz Frederic Rousseau Pascale Zimmermann
author_facet	Antonio Luis Egea-Jimenez Rodrigo Gallardo Abel Garcia-Pino Ylva Ivarsson Anna Maria Wawrzyniak Rudra Kashyap Remy Loris Joost Schymkowitz Frederic Rousseau Pascale Zimmermann
author_sort	Antonio Luis Egea-Jimenez
title	Frizzled 7 and PIP2 binding by syntenin PDZ2 domain supports Frizzled 7 trafficking and signalling
title_short	Frizzled 7 and PIP2 binding by syntenin PDZ2 domain supports Frizzled 7 trafficking and signalling
title_full	Frizzled 7 and PIP2 binding by syntenin PDZ2 domain supports Frizzled 7 trafficking and signalling
title_fullStr	Frizzled 7 and PIP2 binding by syntenin PDZ2 domain supports Frizzled 7 trafficking and signalling
title_full_unstemmed	Frizzled 7 and PIP2 binding by syntenin PDZ2 domain supports Frizzled 7 trafficking and signalling
title_sort	frizzled 7 and pip2 binding by syntenin pdz2 domain supports frizzled 7 trafficking and signalling
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/6a135f7cced44db1b5f72b08dd72540d
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Frizzled 7 and PIP2 binding by syntenin PDZ2 domain supports Frizzled 7 trafficking and signalling

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