Structural basis for adhesion G protein-coupled receptor Gpr126 function

The extracellular regions (ECRs) of adhesion GPCRs have diverse biological functions, but their structures and mechanisms of action remain unclear. Here, the authors solve the ECR structure of the Gpr126 receptor and show that ECR conformation and signaling functions are regulated by alternative spl...

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Autores principales: Katherine Leon, Rebecca L. Cunningham, Joshua A. Riback, Ezra Feldman, Jingxian Li, Tobin R. Sosnick, Minglei Zhao, Kelly R. Monk, Demet Araç
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/e5359c615ebc4086814c00727386b7d8
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spelling oai:doaj.org-article:e5359c615ebc4086814c00727386b7d82021-12-02T17:31:24ZStructural basis for adhesion G protein-coupled receptor Gpr126 function10.1038/s41467-019-14040-12041-1723https://doaj.org/article/e5359c615ebc4086814c00727386b7d82020-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-14040-1https://doaj.org/toc/2041-1723The extracellular regions (ECRs) of adhesion GPCRs have diverse biological functions, but their structures and mechanisms of action remain unclear. Here, the authors solve the ECR structure of the Gpr126 receptor and show that ECR conformation and signaling functions are regulated by alternative splicing.Katherine LeonRebecca L. CunninghamJoshua A. RibackEzra FeldmanJingxian LiTobin R. SosnickMinglei ZhaoKelly R. MonkDemet AraçNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Katherine Leon
Rebecca L. Cunningham
Joshua A. Riback
Ezra Feldman
Jingxian Li
Tobin R. Sosnick
Minglei Zhao
Kelly R. Monk
Demet Araç
Structural basis for adhesion G protein-coupled receptor Gpr126 function
description The extracellular regions (ECRs) of adhesion GPCRs have diverse biological functions, but their structures and mechanisms of action remain unclear. Here, the authors solve the ECR structure of the Gpr126 receptor and show that ECR conformation and signaling functions are regulated by alternative splicing.
format article
author Katherine Leon
Rebecca L. Cunningham
Joshua A. Riback
Ezra Feldman
Jingxian Li
Tobin R. Sosnick
Minglei Zhao
Kelly R. Monk
Demet Araç
author_facet Katherine Leon
Rebecca L. Cunningham
Joshua A. Riback
Ezra Feldman
Jingxian Li
Tobin R. Sosnick
Minglei Zhao
Kelly R. Monk
Demet Araç
author_sort Katherine Leon
title Structural basis for adhesion G protein-coupled receptor Gpr126 function
title_short Structural basis for adhesion G protein-coupled receptor Gpr126 function
title_full Structural basis for adhesion G protein-coupled receptor Gpr126 function
title_fullStr Structural basis for adhesion G protein-coupled receptor Gpr126 function
title_full_unstemmed Structural basis for adhesion G protein-coupled receptor Gpr126 function
title_sort structural basis for adhesion g protein-coupled receptor gpr126 function
publisher Nature Portfolio
publishDate 2020
url https://doaj.org/article/e5359c615ebc4086814c00727386b7d8
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