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dc.contributor.author
Wu, Xu N.
dc.contributor.author
Chu, Liangcui
dc.contributor.author
Xi, Lin
dc.contributor.author
Pertl-Obermeyer, Heidi
dc.contributor.author
Li, Zhi
dc.contributor.author
Sklodowski, Kamil
dc.contributor.author
Sánchez-Rodríguez, Clara
dc.contributor.author
Obermeyer, Gerhard
dc.contributor.author
Schulze, Waltraud X.
dc.date.accessioned
2019-08-19T08:50:16Z
dc.date.available
2019-08-19T06:58:17Z
dc.date.available
2019-08-19T08:50:16Z
dc.date.issued
2019-08
dc.identifier.issn
1535-9476
dc.identifier.issn
1535-9484
dc.identifier.other
10.1074/mcp.ra119.001336
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/359162
dc.identifier.doi
10.3929/ethz-b-000359162
dc.description.abstract
Sucrose as a product of photosynthesis is the major carbohydrate translocated from photosynthetic leaves to growing nonphotosynthetic organs such as roots and seeds. These growing tissues, besides carbohydrate supply, require uptake of water through aquaporins to enhance cell expansion during growth. Previous work revealed Sucrose Induced Receptor Kinase, SIRK1, to control aquaporin activity via phosphorylation in response to external sucrose stimulation. Here, we present the regulatory role of AT3G02880 (QSK1), a receptor kinase with a short external domain, in modulation of SIRK1 activity. Our results suggest that SIRK1 autophosphorylates at Ser-744 after sucrose treatment. Autophosphorylated SIRK1 then interacts with and transphosphorylates QSK1 and QSK2. Upon interaction with QSK1, SIRK1 phosphorylates aquaporins at their regulatory C-terminal phosphorylation sites. Consequently, in root protoplast swelling assays, the qsk1qsk2 mutant showed reduced water influx rates under iso-osmotic sucrose stimulation, confirming an involvement in the same signaling pathway as the receptor kinase SIRK1. Large-scale phosphoproteomics comparing single mutant sirk1, qsk1, and double mutant sirk1 qsk1 revealed that aquaporins were regulated by phosphorylation depending on an activated receptor kinase complex of SIRK1, as well as QSK1. QSK1 thereby acts as a coreceptor stabilizing and enhancing SIRK1 activity and recruiting substrate proteins, such as aquaporins.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
American Society for Biochemistry and Molecular Biology
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.title
Sucrose-induced Receptor Kinase 1 is Modulated by an Interacting Kinase with Short Extracellular Domain
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
dc.date.published
2019-05-30
ethz.journal.title
Molecular & Cellular Proteomics
ethz.journal.volume
18
en_US
ethz.journal.issue
8
en_US
ethz.journal.abbreviated
Mol. cell. proteom.
ethz.pages.start
1556
en_US
ethz.pages.end
1571
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.publication.place
Bethesda, MD
en_US
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02541 - Institut für Molekulare Pflanzenbiologie / Institute of Molecular Plant Biology::09530 - Sánchez-Rodríguez, Clara (ehemalig) / Sánchez-Rodríguez, Clara (former)
en_US
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02541 - Institut für Molekulare Pflanzenbiologie / Institute of Molecular Plant Biology::09530 - Sánchez-Rodríguez, Clara (ehemalig) / Sánchez-Rodríguez, Clara (former)
en_US
ethz.date.deposited
2019-08-19T06:58:25Z
ethz.source
FORM
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2019-08-19T08:50:28Z
ethz.rosetta.lastUpdated
2024-02-02T08:44:01Z
ethz.rosetta.versionExported
true
ethz.COinS
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