A1 Refereed original research article in a scientific journal
The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3
Authors: Sanchez-Barrena, Maria Jose; Fujii, Hiroaki; Angulo, Ivan; Martinez-Ripoll, Martin; Zhu, Jian-Kang; Albert, Armando
Publisher: CELL PRESS
Publishing place: CAMBRIDGE
Publication year: 2007
Journal: Molecular Cell
Journal name in source: MOLECULAR CELL
Journal acronym: MOL CELL
Volume: 26
Issue: 3
First page : 427
Last page: 435
Number of pages: 9
ISSN: 1097-2765
eISSN: 1097-4164
DOI: https://doi.org/10.1016/j.molcel.2007.04.013
Abstract
The plant SOS2 family of protein kinases and their interacting activators, the SOS3 family of calcium-binding proteins, function together in decoding calcium signals elicited by different environmental stimuli. SOS2 is activated by Ca-SOS3 and subsequently phosphorylates the ion transporter SOS1 to bring about cellular ion homeostasis under salt stress. In addition to possessing the kinase activity, members of the SOS2 family of protein kinases can bind to protein phosphatase 2Cs. The crystal structure of the binary complex of Ca-SOS3 with the C-terminal regulatory moiety of SOS2 resolves central questions regarding the dual function of SOS2 as a kinase and a phosphatase-binding protein. A comparison with the structure of unbound SOS3 reveals the basis of the molecular function of this family of kinases and their interacting calcium sensors. Furthermore, our study suggests that the structure of the phosphatase-interaction domain of SOS2 defines a scaffold module conserved from yeast to human.
The plant SOS2 family of protein kinases and their interacting activators, the SOS3 family of calcium-binding proteins, function together in decoding calcium signals elicited by different environmental stimuli. SOS2 is activated by Ca-SOS3 and subsequently phosphorylates the ion transporter SOS1 to bring about cellular ion homeostasis under salt stress. In addition to possessing the kinase activity, members of the SOS2 family of protein kinases can bind to protein phosphatase 2Cs. The crystal structure of the binary complex of Ca-SOS3 with the C-terminal regulatory moiety of SOS2 resolves central questions regarding the dual function of SOS2 as a kinase and a phosphatase-binding protein. A comparison with the structure of unbound SOS3 reveals the basis of the molecular function of this family of kinases and their interacting calcium sensors. Furthermore, our study suggests that the structure of the phosphatase-interaction domain of SOS2 defines a scaffold module conserved from yeast to human.
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