Distinct Roles of N-Terminal Fatty Acid Acylation of the Salinity-Sensor Protein SOS3
| Autor: | Raul Carranco, Dámaso Hornero-Méndez, Elena Fernández García, José M. Pardo, Karin Schumacher, Carlos Tello, Zaida Andrés, Irene Villalta, Francisco J. Quintero, Imelda Mendoza, Anna de Luca |
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| Přispěvatelé: | Junta de Andalucía, Agencia Estatal de Investigación (España) |
| Rok vydání: | 2021 |
| Předmět: |
chemistry.chemical_classification
biology Sodium salt-overly-sensitive pathway Plant culture Fatty acid chemistry.chemical_element Plant Science biology.organism_classification salinity tolerance SB1-1110 Cell biology nuclear entry Acylation Protein acylation SOS3/CBL4 chemistry Arabidopsis Nuclear transport protein acylation Protein kinase A Original Research Calcium signaling |
| Zdroj: | Frontiers in Plant Science, Vol 12 (2021) Frontiers in Plant Science Digital.CSIC. Repositorio Institucional del CSIC instname |
| ISSN: | 1664-462X |
| DOI: | 10.3389/fpls.2021.691124 |
| Popis: | 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 |
| Databáze: | OpenAIRE |
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