Activation of the plasma membrane Na/H antiporter salt-overly-sensitive 1 (SOS1) by phosphorylation of an auto-inhibitory C-terminal domain

Activation of the plasma membrane Na/H antiporter salt-overly-sensitive 1 (SOS1) by phosphorylation of an auto-inhibitory C-terminal domain

Quintero et al.-- 6 páginas, 4 figuras, 25 referencias y 4 páginas adicionales con 5 figuras y 2 tablas.

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Bibliographic Details
Main Authors: Quintero, Francisco J., Martínez-Atienza, Juliana, Villalta, Irene, Mendoza, Imelda, Pardo, José M.
Other Authors: Ministerio de Ciencia e Innovación (España)
Format: artículo biblioteca
Language:English
Published: National Academy of Sciences (U.S.) 2011-01
Subjects:Ion transport, Salinity, Spdium tolerance,
Online Access:http://hdl.handle.net/10261/37957
http://dx.doi.org/10.13039/501100004837
http://dx.doi.org/10.13039/501100000780
http://dx.doi.org/10.13039/100000002
http://dx.doi.org/10.13039/501100004085
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spelling dig-irnas-es-10261-379572021-12-28T16:38:39Z Activation of the plasma membrane Na/H antiporter salt-overly-sensitive 1 (SOS1) by phosphorylation of an auto-inhibitory C-terminal domain Quintero, Francisco J. Martínez-Atienza, Juliana Villalta, Irene Mendoza, Imelda Pardo, José M. Ministerio de Ciencia e Innovación (España) European Commission National Institutes of Health (US) Ministry of Education, Science and Technology (South Korea) Ion transport Salinity Spdium tolerance Quintero et al.-- 6 páginas, 4 figuras, 25 referencias y 4 páginas adicionales con 5 figuras y 2 tablas. The plasma membrane sodium/proton exchanger Salt-Overly-Sensitive 1 (SOS1) is a critical salt tolerance determinant in plants. The SOS2-SOS3 calcium-dependent protein kinase complex up-regulates SOS1 activity, but the mechanistic details of this crucial event remain unresolved. Here we show that SOS1 is maintained in a resting state by a C-terminal auto-inhibitory domain that is the target of SOS2-SOS3. The auto-inhibitory domain interacts intramolecularly with an adjacent domain of SOS1 that is essential for activity. SOS1 is relieved from auto-inhibition upon phosphorylation of the auto-inhibitory domain by SOS2-SOS3. Mutation of the SOS2 phosphorylation and recognition site impeded the activation of SOS1 in vivo and in vitro. Additional amino acid residues critically important for SOS1 activity and regulation were identified in a genetic screen for hypermorphic alleles. This work was supported by Grants BIO2009-08641 and CSD2007-00057 from the Ministerio de Ciencia e Innovación (cofinanced by Fondo Europeo de Desarrollo Regional) (to J.M.P. and F.J.Q.), World Class University Program Grant R32-10148 (to D.-J.Y. and W.Y.K.), and National Institutes of Health Grants R01GM070795 and R01GM059138 (to J.-K.Z.). Peer reviewed 2011-07-24T19:30:38Z 2011-07-24T19:30:38Z 2011-01 artículo http://purl.org/coar/resource_type/c_6501 Proceedings of the National Academy of Sciences of the USA 108 (6): 2611-2616 (2011) 0027-8424 http://hdl.handle.net/10261/37957 10.1073/pnas.1018921108 http://dx.doi.org/10.13039/501100004837 http://dx.doi.org/10.13039/501100000780 http://dx.doi.org/10.13039/100000002 http://dx.doi.org/10.13039/501100004085 21262798 en http://dx.doi.org/10.1073/pnas.1018921108 open National Academy of Sciences (U.S.)
institution IRNAS ES
collection DSpace
country España
countrycode ES
component Bibliográfico
access En linea
databasecode dig-irnas-es
tag biblioteca
region Europa del Sur
libraryname Biblioteca del IRNAS España
language English
topic Ion transport
Salinity
Spdium tolerance
Ion transport
Salinity
Spdium tolerance
spellingShingle Ion transport
Salinity
Spdium tolerance
Ion transport
Salinity
Spdium tolerance
Quintero, Francisco J.
Martínez-Atienza, Juliana
Villalta, Irene
Mendoza, Imelda
Pardo, José M.
Activation of the plasma membrane Na/H antiporter salt-overly-sensitive 1 (SOS1) by phosphorylation of an auto-inhibitory C-terminal domain
description Quintero et al.-- 6 páginas, 4 figuras, 25 referencias y 4 páginas adicionales con 5 figuras y 2 tablas.
author2 Ministerio de Ciencia e Innovación (España)
author_facet Ministerio de Ciencia e Innovación (España)
Quintero, Francisco J.
Martínez-Atienza, Juliana
Villalta, Irene
Mendoza, Imelda
Pardo, José M.
format artículo
topic_facet Ion transport
Salinity
Spdium tolerance
author Quintero, Francisco J.
Martínez-Atienza, Juliana
Villalta, Irene
Mendoza, Imelda
Pardo, José M.
author_sort Quintero, Francisco J.
title Activation of the plasma membrane Na/H antiporter salt-overly-sensitive 1 (SOS1) by phosphorylation of an auto-inhibitory C-terminal domain
title_short Activation of the plasma membrane Na/H antiporter salt-overly-sensitive 1 (SOS1) by phosphorylation of an auto-inhibitory C-terminal domain
title_full Activation of the plasma membrane Na/H antiporter salt-overly-sensitive 1 (SOS1) by phosphorylation of an auto-inhibitory C-terminal domain
title_fullStr Activation of the plasma membrane Na/H antiporter salt-overly-sensitive 1 (SOS1) by phosphorylation of an auto-inhibitory C-terminal domain
title_full_unstemmed Activation of the plasma membrane Na/H antiporter salt-overly-sensitive 1 (SOS1) by phosphorylation of an auto-inhibitory C-terminal domain
title_sort activation of the plasma membrane na/h antiporter salt-overly-sensitive 1 (sos1) by phosphorylation of an auto-inhibitory c-terminal domain
publisher National Academy of Sciences (U.S.)
publishDate 2011-01
url http://hdl.handle.net/10261/37957
http://dx.doi.org/10.13039/501100004837
http://dx.doi.org/10.13039/501100000780
http://dx.doi.org/10.13039/100000002
http://dx.doi.org/10.13039/501100004085
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