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

• Verfasst von: Villalta, Irene [VerfasserIn]
• Verfasst von: García, Elena [VerfasserIn]
• Verfasst von: Hornero-Mendez, Dámaso [VerfasserIn]
• Verfasst von: Carranco, Raúl [VerfasserIn]
• Verfasst von: Tello, Carlos [VerfasserIn]
• Verfasst von: Mendoza, Imelda [VerfasserIn]
• Verfasst von: De Luca, Anna [VerfasserIn]
• Verfasst von: Andrés González, Zaida [VerfasserIn]
• Verfasst von: Schumacher, Karin [VerfasserIn]
• Verfasst von: Pardo, José M. [VerfasserIn]
• Verfasst von: Quintero, Francisco J. [VerfasserIn]
• Titel: Distinct roles of N-terminal fatty acid acylation of the Salinity-sensor protein SOS3
• Verf.angabe: 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
• E-Jahr: 2021
• Jahr: 23 September 2021
• Umfang: 15 S.
• Fussnoten: Gesehen am 23.11.2021
• Titel Quelle: Enthalten in: Frontiers in plant science
• Ort Quelle: Lausanne : Frontiers Media, 2010
• Jahr Quelle: 2021
• Band/Heft Quelle: 12(2021), Artikel-ID 1993, Seite 1-15
• ISSN Quelle: 1664-462X
• DOI: doi:10.3389/fpls.2021.691124
• Datenträger: Online-Ressource
• Sprache: eng
• K10plus-PPN: 1778375758

Abstract

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.