Cyclic nucleotide dependent dephosphorylation of regulator of G-protein signaling 18 in human platelets.

Regulator of G-protein signaling 18 (RGS18) is a GTPase-activating protein that turns off Gq signaling in platelets. RGS18 is regulated by binding to the adaptor protein 14-3-3 via phosphorylated serine residues S49 and S218 on RGS18. In this study we confirm that thrombin, thromboxane A2, or ADP st...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Kristina Gegenbauer, Zoltan Nagy, Albert Smolenski
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/acd9242442494ee2b89a8b6f3631abe1
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:acd9242442494ee2b89a8b6f3631abe1
record_format	dspace
spelling	oai:doaj.org-article:acd9242442494ee2b89a8b6f3631abe12021-11-18T08:47:50ZCyclic nucleotide dependent dephosphorylation of regulator of G-protein signaling 18 in human platelets.1932-620310.1371/journal.pone.0080251https://doaj.org/article/acd9242442494ee2b89a8b6f3631abe12013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24244663/?tool=EBIhttps://doaj.org/toc/1932-6203Regulator of G-protein signaling 18 (RGS18) is a GTPase-activating protein that turns off Gq signaling in platelets. RGS18 is regulated by binding to the adaptor protein 14-3-3 via phosphorylated serine residues S49 and S218 on RGS18. In this study we confirm that thrombin, thromboxane A2, or ADP stimulate the interaction of RGS18 and 14-3-3 by increasing the phosphorylation of S49. Cyclic AMP- and cyclic GMP-dependent kinases (PKA, PKG) inhibit the interaction of RGS18 and 14-3-3 by phosphorylating S216. To understand the effect of S216 phosphorylation we studied the phosphorylation kinetics of S49, S216, and S218 using Phos-tag gels and phosphorylation site-specific antibodies in transfected cells and in platelets. Cyclic nucleotide-induced detachment of 14-3-3 from RGS18 coincides initially with double phosphorylation of S216 and S218. This is followed by dephosphorylation of S49 and S218. Dephosphorylation of S49 and S218 might be mediated by protein phosphatase 1 (PP1) which is linked to RGS18 by the regulatory subunit PPP1R9B (spinophilin). We conclude that PKA and PKG induced S216 phosphorylation triggers the dephosphorylation of the 14-3-3 binding sites of RGS18 in platelets.Kristina GegenbauerZoltan NagyAlbert SmolenskiPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 11, p e80251 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Kristina Gegenbauer Zoltan Nagy Albert Smolenski Cyclic nucleotide dependent dephosphorylation of regulator of G-protein signaling 18 in human platelets.
description	Regulator of G-protein signaling 18 (RGS18) is a GTPase-activating protein that turns off Gq signaling in platelets. RGS18 is regulated by binding to the adaptor protein 14-3-3 via phosphorylated serine residues S49 and S218 on RGS18. In this study we confirm that thrombin, thromboxane A2, or ADP stimulate the interaction of RGS18 and 14-3-3 by increasing the phosphorylation of S49. Cyclic AMP- and cyclic GMP-dependent kinases (PKA, PKG) inhibit the interaction of RGS18 and 14-3-3 by phosphorylating S216. To understand the effect of S216 phosphorylation we studied the phosphorylation kinetics of S49, S216, and S218 using Phos-tag gels and phosphorylation site-specific antibodies in transfected cells and in platelets. Cyclic nucleotide-induced detachment of 14-3-3 from RGS18 coincides initially with double phosphorylation of S216 and S218. This is followed by dephosphorylation of S49 and S218. Dephosphorylation of S49 and S218 might be mediated by protein phosphatase 1 (PP1) which is linked to RGS18 by the regulatory subunit PPP1R9B (spinophilin). We conclude that PKA and PKG induced S216 phosphorylation triggers the dephosphorylation of the 14-3-3 binding sites of RGS18 in platelets.
format	article
author	Kristina Gegenbauer Zoltan Nagy Albert Smolenski
author_facet	Kristina Gegenbauer Zoltan Nagy Albert Smolenski
author_sort	Kristina Gegenbauer
title	Cyclic nucleotide dependent dephosphorylation of regulator of G-protein signaling 18 in human platelets.
title_short	Cyclic nucleotide dependent dephosphorylation of regulator of G-protein signaling 18 in human platelets.
title_full	Cyclic nucleotide dependent dephosphorylation of regulator of G-protein signaling 18 in human platelets.
title_fullStr	Cyclic nucleotide dependent dephosphorylation of regulator of G-protein signaling 18 in human platelets.
title_full_unstemmed	Cyclic nucleotide dependent dephosphorylation of regulator of G-protein signaling 18 in human platelets.
title_sort	cyclic nucleotide dependent dephosphorylation of regulator of g-protein signaling 18 in human platelets.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/acd9242442494ee2b89a8b6f3631abe1
work_keys_str_mv	AT kristinagegenbauer cyclicnucleotidedependentdephosphorylationofregulatorofgproteinsignaling18inhumanplatelets AT zoltannagy cyclicnucleotidedependentdephosphorylationofregulatorofgproteinsignaling18inhumanplatelets AT albertsmolenski cyclicnucleotidedependentdephosphorylationofregulatorofgproteinsignaling18inhumanplatelets
_version_	1718421342447992832

Cyclic nucleotide dependent dephosphorylation of regulator of G-protein signaling 18 in human platelets.

Ejemplares similares