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Sucrose-induced Receptor Kinase 1 is Modulated by an Interacting Kinase with Short Extracellular Domain
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...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Biochemistry and Molecular Biology
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6683012/ https://www.ncbi.nlm.nih.gov/pubmed/31147492 http://dx.doi.org/10.1074/mcp.RA119.001336 |
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author | Wu, Xu Na Chu, Liangcui Xi, Lin Pertl-Obermeyer, Heidi Li, Zhi Sklodowski, Kamil Sanchez-Rodriguez, Clara Obermeyer, Gerhard Schulze, Waltraud X. |
author_facet | Wu, Xu Na Chu, Liangcui Xi, Lin Pertl-Obermeyer, Heidi Li, Zhi Sklodowski, Kamil Sanchez-Rodriguez, Clara Obermeyer, Gerhard Schulze, Waltraud X. |
author_sort | Wu, Xu Na |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-6683012 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | The American Society for Biochemistry and Molecular Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-66830122019-08-07 Sucrose-induced Receptor Kinase 1 is Modulated by an Interacting Kinase with Short Extracellular Domain Wu, Xu Na Chu, Liangcui Xi, Lin Pertl-Obermeyer, Heidi Li, Zhi Sklodowski, Kamil Sanchez-Rodriguez, Clara Obermeyer, Gerhard Schulze, Waltraud X. Mol Cell Proteomics Research 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. The American Society for Biochemistry and Molecular Biology 2019-08 2019-05-30 /pmc/articles/PMC6683012/ /pubmed/31147492 http://dx.doi.org/10.1074/mcp.RA119.001336 Text en © 2019 Wu et al. Published by The American Society for Biochemistry and Molecular Biology, Inc. Author's Choice—Final version open access under the terms of the Creative Commons CC-BY license (http://creativecommons.org/licenses/by/4.0) . |
spellingShingle | Research Wu, Xu Na Chu, Liangcui Xi, Lin Pertl-Obermeyer, Heidi Li, Zhi Sklodowski, Kamil Sanchez-Rodriguez, Clara Obermeyer, Gerhard Schulze, Waltraud X. Sucrose-induced Receptor Kinase 1 is Modulated by an Interacting Kinase with Short Extracellular Domain |
title | Sucrose-induced Receptor Kinase 1 is Modulated by an Interacting Kinase with Short Extracellular Domain |
title_full | Sucrose-induced Receptor Kinase 1 is Modulated by an Interacting Kinase with Short Extracellular Domain |
title_fullStr | Sucrose-induced Receptor Kinase 1 is Modulated by an Interacting Kinase with Short Extracellular Domain |
title_full_unstemmed | Sucrose-induced Receptor Kinase 1 is Modulated by an Interacting Kinase with Short Extracellular Domain |
title_short | Sucrose-induced Receptor Kinase 1 is Modulated by an Interacting Kinase with Short Extracellular Domain |
title_sort | sucrose-induced receptor kinase 1 is modulated by an interacting kinase with short extracellular domain |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6683012/ https://www.ncbi.nlm.nih.gov/pubmed/31147492 http://dx.doi.org/10.1074/mcp.RA119.001336 |
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