Molecular basis for the binding and selective dephosphorylation of Na+/H+ exchanger 1 by calcineurin

The mechanism by which Ser/Thr protein phosphatases specifically recruit and dephosphorylate their substrates is largely unclear. Hear, the authors elucidate how the Ser/Thr protein phosphatase calcineurin is recruited to its substrate NHE1 and how site-specific dephosphorylation is achieved.

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Autores principales:	Ruth Hendus-Altenburger, Xinru Wang, Lise M. Sjøgaard-Frich, Elena Pedraz-Cuesta, Sarah R. Sheftic, Anne H. Bendsøe, Rebecca Page, Birthe B. Kragelund, Stine F. Pedersen, Wolfgang Peti
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/5e565aa376cd44bab46f43a617043caa
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spelling	oai:doaj.org-article:5e565aa376cd44bab46f43a617043caa2021-12-02T15:35:48ZMolecular basis for the binding and selective dephosphorylation of Na+/H+ exchanger 1 by calcineurin10.1038/s41467-019-11391-72041-1723https://doaj.org/article/5e565aa376cd44bab46f43a617043caa2019-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-11391-7https://doaj.org/toc/2041-1723The mechanism by which Ser/Thr protein phosphatases specifically recruit and dephosphorylate their substrates is largely unclear. Hear, the authors elucidate how the Ser/Thr protein phosphatase calcineurin is recruited to its substrate NHE1 and how site-specific dephosphorylation is achieved.Ruth Hendus-AltenburgerXinru WangLise M. Sjøgaard-FrichElena Pedraz-CuestaSarah R. ShefticAnne H. BendsøeRebecca PageBirthe B. KragelundStine F. PedersenWolfgang PetiNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Ruth Hendus-Altenburger Xinru Wang Lise M. Sjøgaard-Frich Elena Pedraz-Cuesta Sarah R. Sheftic Anne H. Bendsøe Rebecca Page Birthe B. Kragelund Stine F. Pedersen Wolfgang Peti Molecular basis for the binding and selective dephosphorylation of Na+/H+ exchanger 1 by calcineurin
description	The mechanism by which Ser/Thr protein phosphatases specifically recruit and dephosphorylate their substrates is largely unclear. Hear, the authors elucidate how the Ser/Thr protein phosphatase calcineurin is recruited to its substrate NHE1 and how site-specific dephosphorylation is achieved.
format	article
author	Ruth Hendus-Altenburger Xinru Wang Lise M. Sjøgaard-Frich Elena Pedraz-Cuesta Sarah R. Sheftic Anne H. Bendsøe Rebecca Page Birthe B. Kragelund Stine F. Pedersen Wolfgang Peti
author_facet	Ruth Hendus-Altenburger Xinru Wang Lise M. Sjøgaard-Frich Elena Pedraz-Cuesta Sarah R. Sheftic Anne H. Bendsøe Rebecca Page Birthe B. Kragelund Stine F. Pedersen Wolfgang Peti
author_sort	Ruth Hendus-Altenburger
title	Molecular basis for the binding and selective dephosphorylation of Na+/H+ exchanger 1 by calcineurin
title_short	Molecular basis for the binding and selective dephosphorylation of Na+/H+ exchanger 1 by calcineurin
title_full	Molecular basis for the binding and selective dephosphorylation of Na+/H+ exchanger 1 by calcineurin
title_fullStr	Molecular basis for the binding and selective dephosphorylation of Na+/H+ exchanger 1 by calcineurin
title_full_unstemmed	Molecular basis for the binding and selective dephosphorylation of Na+/H+ exchanger 1 by calcineurin
title_sort	molecular basis for the binding and selective dephosphorylation of na+/h+ exchanger 1 by calcineurin
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/5e565aa376cd44bab46f43a617043caa
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Molecular basis for the binding and selective dephosphorylation of Na+/H+ exchanger 1 by calcineurin

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