The Ly6 protein coiled is required for septate junction and blood brain barrier organisation in Drosophila.

<h4>Background</h4>Genetic analysis of the Drosophila septate junctions has greatly contributed to our understanding of the mechanisms controlling the assembly of these adhesion structures, which bear strong similarities with the vertebrate tight junctions and the paranodal septate junct...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Assia Hijazi, Marc Haenlin, Lucas Waltzer, Fernando Roch
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/de2caa52473f482c9bc6f1e2400cbd86
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:de2caa52473f482c9bc6f1e2400cbd86
record_format	dspace
spelling	oai:doaj.org-article:de2caa52473f482c9bc6f1e2400cbd862021-11-18T06:57:19ZThe Ly6 protein coiled is required for septate junction and blood brain barrier organisation in Drosophila.1932-620310.1371/journal.pone.0017763https://doaj.org/article/de2caa52473f482c9bc6f1e2400cbd862011-03-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21423573/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>Genetic analysis of the Drosophila septate junctions has greatly contributed to our understanding of the mechanisms controlling the assembly of these adhesion structures, which bear strong similarities with the vertebrate tight junctions and the paranodal septate junctions. These adhesion complexes share conserved molecular components and have a common function: the formation of paracellular barriers restraining the diffusion of solutes through epithelial and glial envelopes.<h4>Methodology/principal findings</h4>In this work we characterise the function of the Drosophila cold gene, that codes for a protein belonging to the Ly6 superfamily of extracellular ligands. Analysis of cold mutants shows that this gene is specifically required for the organisation of the septate junctions in epithelial tissues and in the nervous system, where its contribution is essential for the maintenance of the blood-brain barrier. We show that cold acts in a cell autonomous way, and we present evidence indicating that this protein could act as a septate junction component.<h4>Conclusion/significance</h4>We discuss the specific roles of cold and three other Drosophila members of the Ly6 superfamily that have been shown to participate in a non-redundant way in the process of septate junction assembly. We propose that vertebrate Ly6 proteins could fulfill analogous roles in tight junctions and/or paranodal septate junctions.Assia HijaziMarc HaenlinLucas WaltzerFernando RochPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 3, p e17763 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Assia Hijazi Marc Haenlin Lucas Waltzer Fernando Roch The Ly6 protein coiled is required for septate junction and blood brain barrier organisation in Drosophila.
description	<h4>Background</h4>Genetic analysis of the Drosophila septate junctions has greatly contributed to our understanding of the mechanisms controlling the assembly of these adhesion structures, which bear strong similarities with the vertebrate tight junctions and the paranodal septate junctions. These adhesion complexes share conserved molecular components and have a common function: the formation of paracellular barriers restraining the diffusion of solutes through epithelial and glial envelopes.<h4>Methodology/principal findings</h4>In this work we characterise the function of the Drosophila cold gene, that codes for a protein belonging to the Ly6 superfamily of extracellular ligands. Analysis of cold mutants shows that this gene is specifically required for the organisation of the septate junctions in epithelial tissues and in the nervous system, where its contribution is essential for the maintenance of the blood-brain barrier. We show that cold acts in a cell autonomous way, and we present evidence indicating that this protein could act as a septate junction component.<h4>Conclusion/significance</h4>We discuss the specific roles of cold and three other Drosophila members of the Ly6 superfamily that have been shown to participate in a non-redundant way in the process of septate junction assembly. We propose that vertebrate Ly6 proteins could fulfill analogous roles in tight junctions and/or paranodal septate junctions.
format	article
author	Assia Hijazi Marc Haenlin Lucas Waltzer Fernando Roch
author_facet	Assia Hijazi Marc Haenlin Lucas Waltzer Fernando Roch
author_sort	Assia Hijazi
title	The Ly6 protein coiled is required for septate junction and blood brain barrier organisation in Drosophila.
title_short	The Ly6 protein coiled is required for septate junction and blood brain barrier organisation in Drosophila.
title_full	The Ly6 protein coiled is required for septate junction and blood brain barrier organisation in Drosophila.
title_fullStr	The Ly6 protein coiled is required for septate junction and blood brain barrier organisation in Drosophila.
title_full_unstemmed	The Ly6 protein coiled is required for septate junction and blood brain barrier organisation in Drosophila.
title_sort	ly6 protein coiled is required for septate junction and blood brain barrier organisation in drosophila.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/de2caa52473f482c9bc6f1e2400cbd86
work_keys_str_mv	AT assiahijazi thely6proteincoiledisrequiredforseptatejunctionandbloodbrainbarrierorganisationindrosophila AT marchaenlin thely6proteincoiledisrequiredforseptatejunctionandbloodbrainbarrierorganisationindrosophila AT lucaswaltzer thely6proteincoiledisrequiredforseptatejunctionandbloodbrainbarrierorganisationindrosophila AT fernandoroch thely6proteincoiledisrequiredforseptatejunctionandbloodbrainbarrierorganisationindrosophila AT assiahijazi ly6proteincoiledisrequiredforseptatejunctionandbloodbrainbarrierorganisationindrosophila AT marchaenlin ly6proteincoiledisrequiredforseptatejunctionandbloodbrainbarrierorganisationindrosophila AT lucaswaltzer ly6proteincoiledisrequiredforseptatejunctionandbloodbrainbarrierorganisationindrosophila AT fernandoroch ly6proteincoiledisrequiredforseptatejunctionandbloodbrainbarrierorganisationindrosophila
_version_	1718424200181448704

The Ly6 protein coiled is required for septate junction and blood brain barrier organisation in Drosophila.

Ejemplares similares