Rice calcium-dependent protein kinase OsCPK17 targets plasma membrane intrinsic protein and sucrose phosphate synthase and is required for a proper cold stress response

Handle URI:
http://hdl.handle.net/10754/622723
Title:
Rice calcium-dependent protein kinase OsCPK17 targets plasma membrane intrinsic protein and sucrose phosphate synthase and is required for a proper cold stress response
Authors:
Almadanim, M. Cecília; Alexandre, Bruno M.; Rosa, Margarida T.G.; Sapeta, Helena; Leitão, António E.; Ramalho, José C.; Lam, TuKiet T.; Negrão, Sónia; Abreu, Isabel A. ( 0000-0002-5566-2146 ) ; Oliveira, M. Margarida
Abstract:
Calcium-dependent protein kinases (CDPKs) are involved in plant tolerance mechanisms to abiotic stresses. Although CDPKs are recognized as key messengers in signal transduction, the specific role of most members of this family remains unknown. Here we test the hypothesis that OsCPK17 plays a role in rice cold stress response by analyzing OsCPK17 knockout, silencing, and overexpressing rice lines under low temperature. Altered OsCPK17 gene expression compromises cold tolerance performance, without affecting the expression of key cold stress-inducible genes. A comparative phosphoproteomic approach led to the identification of six potential in vivo OsCPK17 targets, which are associated with sugar and nitrogen metabolism, and with osmotic regulation. To test direct interaction, in vitro kinase assays were performed, showing that the sucrose phosphate synthase OsSPS4, and the aquaporin OsPIP2;1/OsPIP2;6 are phosphorylated by OsCPK17 in a calcium-dependent manner. Altogether, our data indicates that OsCPK17 is required for a proper cold stress response in rice, likely affecting the activity of membrane channels and sugar metabolism.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division
Citation:
Almadanim MC, Alexandre BM, Rosa MTG, Sapeta H, Leitão AE, et al. (2017) Rice calcium-dependent protein kinase OsCPK17 targets plasma membrane intrinsic protein and sucrose phosphate synthase and is required for a proper cold stress response. Plant, Cell & Environment. Available: http://dx.doi.org/10.1111/pce.12916.
Publisher:
Wiley-Blackwell
Journal:
Plant, Cell & Environment
Issue Date:
19-Jan-2017
DOI:
10.1111/pce.12916
Type:
Article
ISSN:
0140-7791
Sponsors:
We acknowledge: Alexandra Marques for cloning OsCPK17 into pDEST28; Pedro Pereira for the help with the transgenic rice plants; Nuno Gonçalves, Mafalda Rodrigues and Vanessa Azevedo for the aid with electrolyte leakage datapoint sample collection; Tiago Lourenço and Ana Paula Farinha for providing some of the primers used; Margarida Saramago for the support with scintillation counter equipment and borrowed material; Edward Voss, Jean Kanyo, and Kathrin Wilczak for their assistance in MS sample preparation, data collection, and initial data analysis, respectively. We also thank Rossana Henriques (CRAG), Nelson Saibo (ITQB), and Alison Funston (Monash University, Australia) for critical revision. This research was funded by Portuguese Fundação para a Ciência e a Tecnologia: grants SFRH/BD/61121/2009 to M.C.A., SFRH/BD/84219/2012 to M.T.G.R., SFRH/BD/89781/2012 to H.S., SFRH/BPD/98619/2013 to B.M.A.; FCT Investigator (POPH-QREN) to I.A.A.. The work was also supported by the FCT research units GREEN-it
Additional Links:
http://onlinelibrary.wiley.com/doi/10.1111/pce.12916/abstract
Appears in Collections:
Articles; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorAlmadanim, M. Cecíliaen
dc.contributor.authorAlexandre, Bruno M.en
dc.contributor.authorRosa, Margarida T.G.en
dc.contributor.authorSapeta, Helenaen
dc.contributor.authorLeitão, António E.en
dc.contributor.authorRamalho, José C.en
dc.contributor.authorLam, TuKiet T.en
dc.contributor.authorNegrão, Sóniaen
dc.contributor.authorAbreu, Isabel A.en
dc.contributor.authorOliveira, M. Margaridaen
dc.date.accessioned2017-01-24T08:30:07Z-
dc.date.available2017-01-24T08:30:07Z-
dc.date.issued2017-01-19en
dc.identifier.citationAlmadanim MC, Alexandre BM, Rosa MTG, Sapeta H, Leitão AE, et al. (2017) Rice calcium-dependent protein kinase OsCPK17 targets plasma membrane intrinsic protein and sucrose phosphate synthase and is required for a proper cold stress response. Plant, Cell & Environment. Available: http://dx.doi.org/10.1111/pce.12916.en
dc.identifier.issn0140-7791en
dc.identifier.doi10.1111/pce.12916en
dc.identifier.urihttp://hdl.handle.net/10754/622723-
dc.description.abstractCalcium-dependent protein kinases (CDPKs) are involved in plant tolerance mechanisms to abiotic stresses. Although CDPKs are recognized as key messengers in signal transduction, the specific role of most members of this family remains unknown. Here we test the hypothesis that OsCPK17 plays a role in rice cold stress response by analyzing OsCPK17 knockout, silencing, and overexpressing rice lines under low temperature. Altered OsCPK17 gene expression compromises cold tolerance performance, without affecting the expression of key cold stress-inducible genes. A comparative phosphoproteomic approach led to the identification of six potential in vivo OsCPK17 targets, which are associated with sugar and nitrogen metabolism, and with osmotic regulation. To test direct interaction, in vitro kinase assays were performed, showing that the sucrose phosphate synthase OsSPS4, and the aquaporin OsPIP2;1/OsPIP2;6 are phosphorylated by OsCPK17 in a calcium-dependent manner. Altogether, our data indicates that OsCPK17 is required for a proper cold stress response in rice, likely affecting the activity of membrane channels and sugar metabolism.en
dc.description.sponsorshipWe acknowledge: Alexandra Marques for cloning OsCPK17 into pDEST28; Pedro Pereira for the help with the transgenic rice plants; Nuno Gonçalves, Mafalda Rodrigues and Vanessa Azevedo for the aid with electrolyte leakage datapoint sample collection; Tiago Lourenço and Ana Paula Farinha for providing some of the primers used; Margarida Saramago for the support with scintillation counter equipment and borrowed material; Edward Voss, Jean Kanyo, and Kathrin Wilczak for their assistance in MS sample preparation, data collection, and initial data analysis, respectively. We also thank Rossana Henriques (CRAG), Nelson Saibo (ITQB), and Alison Funston (Monash University, Australia) for critical revision. This research was funded by Portuguese Fundação para a Ciência e a Tecnologia: grants SFRH/BD/61121/2009 to M.C.A., SFRH/BD/84219/2012 to M.T.G.R., SFRH/BD/89781/2012 to H.S., SFRH/BPD/98619/2013 to B.M.A.; FCT Investigator (POPH-QREN) to I.A.A.. The work was also supported by the FCT research units GREEN-iten
dc.publisherWiley-Blackwellen
dc.relation.urlhttp://onlinelibrary.wiley.com/doi/10.1111/pce.12916/abstracten
dc.rightsThis is the peer reviewed version of the following article: Almadanim, M. C., Alexandre, B. M., Rosa, M. T. G., Sapeta, H., Leitão, A. E., Ramalho, J. C., Lam, T. T., Negrão, S., Abreu, I. A., and Oliveira, M. M. (2017) \Rice calcium-dependent protein kinase OsCPK17 targets plasma membrane intrinsic protein and sucrose phosphate synthase and is required for a proper cold stress response. Plant, Cell & Environment, doi: 10.1111/pce.12916., which has been published in final form at http://onlinelibrary.wiley.com/doi/10.1111/pce.12916/abstract. This article may be used for non-commercial purposes in accordance With Wiley Terms and Conditions for self-archiving.en
dc.subjectCDPK, abiotic stress, cold stress, signal transduction, phosphoproteomics, phosphorylationen
dc.titleRice calcium-dependent protein kinase OsCPK17 targets plasma membrane intrinsic protein and sucrose phosphate synthase and is required for a proper cold stress responseen
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.identifier.journalPlant, Cell & Environmenten
dc.eprint.versionPost-printen
dc.contributor.institutionInstituto de Tecnologia Química e Biológica António Xavier; Universidade Nova de Lisboa; 2780-157 Oeiras Portugalen
dc.contributor.institutionInstituto de Biologia Experimental e Tecnológica; 2780-157 Oeiras Portugalen
dc.contributor.institutionPlant Stress & Biodiversity, Linking Landscape, Environment, Agriculture, and Food (LEAF), Dept. Recursos Naturais, Ambiente e Território (DRAT); Instituto Superior de Agronomia, Universidade de Lisboa; 2784-505 Oeiras Portugalen
dc.contributor.institutionDepartment of Molecular Biophysics and Biochemistry; Yale University; New Haven CT 06520-8024 USAen
dc.contributor.institutionMS & Proteomics Resource, WM Keck Foundation Biotechnology Resource Laboratory; Yale University; New Haven CT 06520-8024 USAen
kaust.authorNegrão, Sóniaen
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