Mechanistic insights into the role of prenyl-binding protein PrBP/δ in membrane dissociation of phosphodiesterase 6

The prenyl-binding protein PrBP/δ is a solubilization factor involved in trafficking of prenylated proteins. Here the authors present the ligand-free apo-PrBP/δ structure and propose a "solubilization by depletion" mechanism, where PrBP/δ sequesters only soluble rod photoreceptor phosphodi...

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Autores principales:	Bilal M. Qureshi, Andrea Schmidt, Elmar Behrmann, Jörg Bürger, Thorsten Mielke, Christian M. T. Spahn, Martin Heck, Patrick Scheerer
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/ea0ddcb4147a4a1bb7ab1587a5c0208b
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spelling	oai:doaj.org-article:ea0ddcb4147a4a1bb7ab1587a5c0208b2021-12-02T17:33:01ZMechanistic insights into the role of prenyl-binding protein PrBP/δ in membrane dissociation of phosphodiesterase 610.1038/s41467-017-02569-y2041-1723https://doaj.org/article/ea0ddcb4147a4a1bb7ab1587a5c0208b2018-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-02569-yhttps://doaj.org/toc/2041-1723The prenyl-binding protein PrBP/δ is a solubilization factor involved in trafficking of prenylated proteins. Here the authors present the ligand-free apo-PrBP/δ structure and propose a "solubilization by depletion" mechanism, where PrBP/δ sequesters only soluble rod photoreceptor phosphodiesterase (PDE6), leading to a dissociation of membrane-bound PDE6.Bilal M. QureshiAndrea SchmidtElmar BehrmannJörg BürgerThorsten MielkeChristian M. T. SpahnMartin HeckPatrick ScheererNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Bilal M. Qureshi Andrea Schmidt Elmar Behrmann Jörg Bürger Thorsten Mielke Christian M. T. Spahn Martin Heck Patrick Scheerer Mechanistic insights into the role of prenyl-binding protein PrBP/δ in membrane dissociation of phosphodiesterase 6
description	The prenyl-binding protein PrBP/δ is a solubilization factor involved in trafficking of prenylated proteins. Here the authors present the ligand-free apo-PrBP/δ structure and propose a "solubilization by depletion" mechanism, where PrBP/δ sequesters only soluble rod photoreceptor phosphodiesterase (PDE6), leading to a dissociation of membrane-bound PDE6.
format	article
author	Bilal M. Qureshi Andrea Schmidt Elmar Behrmann Jörg Bürger Thorsten Mielke Christian M. T. Spahn Martin Heck Patrick Scheerer
author_facet	Bilal M. Qureshi Andrea Schmidt Elmar Behrmann Jörg Bürger Thorsten Mielke Christian M. T. Spahn Martin Heck Patrick Scheerer
author_sort	Bilal M. Qureshi
title	Mechanistic insights into the role of prenyl-binding protein PrBP/δ in membrane dissociation of phosphodiesterase 6
title_short	Mechanistic insights into the role of prenyl-binding protein PrBP/δ in membrane dissociation of phosphodiesterase 6
title_full	Mechanistic insights into the role of prenyl-binding protein PrBP/δ in membrane dissociation of phosphodiesterase 6
title_fullStr	Mechanistic insights into the role of prenyl-binding protein PrBP/δ in membrane dissociation of phosphodiesterase 6
title_full_unstemmed	Mechanistic insights into the role of prenyl-binding protein PrBP/δ in membrane dissociation of phosphodiesterase 6
title_sort	mechanistic insights into the role of prenyl-binding protein prbp/δ in membrane dissociation of phosphodiesterase 6
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/ea0ddcb4147a4a1bb7ab1587a5c0208b
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Mechanistic insights into the role of prenyl-binding protein PrBP/δ in membrane dissociation of phosphodiesterase 6

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