Cover Image

Distinct roles of N-terminal fatty acid acylation of the Salinity-sensor protein SOS3

The Salt-Overly-Sensitive (SOS) pathway controls the net uptake of sodium by roots and the xylematic transfer to shoots in vascular plants. SOS3/CBL4 is a core component of the SOS pathway that senses calcium signaling of salinity stress to activate and recruit the protein kinase SOS2/CIPK24 to the...

Full description

Saved in:
Bibliographic Details
Main Authors: Villalta, Irene (Author) , García, Elena (Author) , Hornero-Mendez, Dámaso (Author) , Carranco, Raúl (Author) , Tello Lacal, Carlos (Author) , Mendoza, Imelda (Author) , De Luca, Anna (Author) , Andrés González, Zaida (Author) , Schumacher, Karin (Author) , Pardo, José M. (Author) , Quintero, Francisco J. (Author)
Format: Article (Journal)
Language:English
Published: 23 September 2021
In: Frontiers in plant science
Year: 2021, Volume: 12, Pages: 1-15
ISSN:1664-462X
DOI:10.3389/fpls.2021.691124
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.3389/fpls.2021.691124
Verlag, lizenzpflichtig, Volltext: https://www.frontiersin.org/article/10.3389/fpls.2021.691124
Get full text
Author Notes:Irene Villalta, Elena García, Dámaso Hornero-Mendez, Raúl Carranco, Carlos Tello, Imelda Mendoza, Anna De Luca, Zaida Andrés, Karin Schumacher, José M. Pardo and Francisco J. Quintero
Description
Summary:The Salt-Overly-Sensitive (SOS) pathway controls the net uptake of sodium by roots and the xylematic transfer to shoots in vascular plants. SOS3/CBL4 is a core component of the SOS pathway that senses calcium signaling of salinity stress to activate and recruit the protein kinase SOS2/CIPK24 to the plasma membrane to trigger sodium efflux by the Na/H exchanger SOS1/NHX7. However, despite the well-established function of SOS3 at the plasma membrane, SOS3 displays a nucleo-cytoplasmic distribution whose physiological meaning is not understood. Here, we show that the N-terminal part of SOS3 encodes structural information for dual acylation with myristic and palmitic fatty acids, each of which commands a different location and function of SOS3. N-myristoylation at glycine-2 is essential for plasma membrane association and recruiting SOS2 to activate SOS1, whereas S-acylation at cysteine-3 redirects SOS3 toward the nucleus. Moreover, a poly-lysine track in positions 7-11 that is unique to SOS3 among other Arabidopsis CBLs appears to be essential for the correct positioning of the SOS2-SOS3 complex at the plasma membrane for the activation of SOS1. The nuclear-localized SOS3 protein had limited bearing on the salt tolerance of Arabidopsis. These results are evidence of a novel S-acylation dependent nuclear trafficking mechanism that contrasts with alternative subcellular targeting of other CBLs by S-acylation.
Item Description:Gesehen am 23.11.2021
Physical Description:Online Resource
ISSN:1664-462X
DOI:10.3389/fpls.2021.691124

Similar Items