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

Francisco J. Quintero; Juliana Martínez-Atienza; Irene Villalta; Xingyu Jiang; Woeyeon Kim; Zhair Ali; Hiroaki Fujii; Imelda Mendoza; Daejin Yun; Jian-Kang Zhu; José Manuel Pardo

doi:10.1073/pnas.1018921108

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

Francisco J. Quintero, Juliana Martínez-Atienza, Irene Villalta, Xingyu Jiang, Woeyeon Kim, Zhair Ali, Hiroaki Fujii, Imelda Mendoza, Daejin Yun, Jian-Kang Zhu, José Manuel Pardo

Research output: Contribution to journal › Article › peer-review

320 Scopus citations

Abstract

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 upregulates 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.

Original language	English (US)
Pages (from-to)	2611-2616
Number of pages	6
Journal	Proceedings of the National Academy of Sciences
Volume	108
Issue number	6
DOIs	https://doi.org/10.1073/pnas.1018921108
State	Published - Jan 24 2011

Bibliographical note

KAUST Repository Item: Exported on 2020-10-01
Acknowledgements: We are indebted to Unidad de Proteomica, Centro Nacional de Investigaciones Cardiovasculares Carlos III, for mass-spectrometric analysis. This work was supported by Grants BIO2009-08641 and CSD2007-00057 from the Ministerio de Ciencia e Innovacion (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.).

ASJC Scopus subject areas

General

Access to Document

10.1073/pnas.1018921108

Cite this

Quintero, F. J., Martínez-Atienza, J., Villalta, I., Jiang, X., Kim, W., Ali, Z., Fujii, H., Mendoza, I., Yun, D., Zhu, J.-K., & Pardo, J. M. (2011). Activation of the plasma membrane Na/H antiporter salt-overly-sensitive 1 (SOS1) by phosphorylation of an auto-inhibitory C-terminal domain. Proceedings of the National Academy of Sciences, 108(6), 2611-2616. https://doi.org/10.1073/pnas.1018921108

@article{a35fa31c9cbe490e9a558aa6a5f2ef05,

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

abstract = "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 upregulates 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.",

author = "Quintero, {Francisco J.} and Juliana Mart{\'i}nez-Atienza and Irene Villalta and Xingyu Jiang and Woeyeon Kim and Zhair Ali and Hiroaki Fujii and Imelda Mendoza and Daejin Yun and Jian-Kang Zhu and Pardo, {Jos{\'e} Manuel}",

note = "KAUST Repository Item: Exported on 2020-10-01 Acknowledgements: We are indebted to Unidad de Proteomica, Centro Nacional de Investigaciones Cardiovasculares Carlos III, for mass-spectrometric analysis. This work was supported by Grants BIO2009-08641 and CSD2007-00057 from the Ministerio de Ciencia e Innovacion (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.).",

year = "2011",

month = jan,

day = "24",

doi = "10.1073/pnas.1018921108",

language = "English (US)",

volume = "108",

pages = "2611--2616",

journal = "Proceedings of the National Academy of Sciences",

issn = "0027-8424",

publisher = "National Academy of Sciences",

number = "6",

}

Quintero, FJ, Martínez-Atienza, J, Villalta, I, Jiang, X, Kim, W, Ali, Z, Fujii, H, Mendoza, I, Yun, D, Zhu, J-K & Pardo, JM 2011, 'Activation of the plasma membrane Na/H antiporter salt-overly-sensitive 1 (SOS1) by phosphorylation of an auto-inhibitory C-terminal domain', Proceedings of the National Academy of Sciences, vol. 108, no. 6, pp. 2611-2616. https://doi.org/10.1073/pnas.1018921108

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 et al.
In: Proceedings of the National Academy of Sciences, Vol. 108, No. 6, 24.01.2011, p. 2611-2616.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Activation of the plasma membrane Na/H antiporter salt-overly-sensitive 1 (SOS1) by phosphorylation of an auto-inhibitory C-terminal domain

AU - Quintero, Francisco J.

AU - Martínez-Atienza, Juliana

AU - Villalta, Irene

AU - Jiang, Xingyu

AU - Kim, Woeyeon

AU - Ali, Zhair

AU - Fujii, Hiroaki

AU - Mendoza, Imelda

AU - Yun, Daejin

AU - Zhu, Jian-Kang

AU - Pardo, José Manuel

N1 - KAUST Repository Item: Exported on 2020-10-01 Acknowledgements: We are indebted to Unidad de Proteomica, Centro Nacional de Investigaciones Cardiovasculares Carlos III, for mass-spectrometric analysis. This work was supported by Grants BIO2009-08641 and CSD2007-00057 from the Ministerio de Ciencia e Innovacion (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.).

PY - 2011/1/24

Y1 - 2011/1/24

N2 - 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 upregulates 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.

AB - 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 upregulates 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.

UR - http://hdl.handle.net/10754/561705

UR - http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3038701

UR - http://www.scopus.com/inward/record.url?scp=79952298500&partnerID=8YFLogxK

U2 - 10.1073/pnas.1018921108

DO - 10.1073/pnas.1018921108

M3 - Article

C2 - 21262798

SN - 0027-8424

VL - 108

SP - 2611

EP - 2616

JO - Proceedings of the National Academy of Sciences

JF - Proceedings of the National Academy of Sciences

IS - 6

ER -

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

Abstract

Bibliographical note

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this