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...
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| Main Authors: | , , , , , , , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
23 September 2021
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| 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 
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| 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 |
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| 520 | |a 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. | ||
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