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Title

Multiple protein modifications of SOS3/CBL4 regulate subcellular localization and interaction with protein partners involved in salt tolerance

AuthorsPardo, José M. ; Villalta, Irene ; García-Martín, Elena; Quintero, Francisco J.
Issue Date7-May-2014
PublisherDeutsche Forschungsgemeinschaft
CitationPlant Primary Metabolism: Synthesis, Storage and Degradation Processes. FOR1061 International Meeting, Heidelberg 7-9 mayo 2014 (Germany)
AbstractCalcineurin B-like proteins (CBLs) are a family of calcium sensor proteins that interact with SnRK3 serine-threonine kinases, also known as CBL-interacting protein kinases (CIPKs). CBl-CIPK complexes relay signals that regulate ion fluxes and sustain plant responses to environmental cues. CBL4/S0S3. logether with CIPK24/S0S2 and the Na/H exehanger SOS1, are key regulalors of salt tolerance in plants. Besides calcium binding, SOS3 is subjected to and array of post-translational modifications that regulate membrane targeting and the interaction with the SOS2 and SOS1 partners. Known modifications include phosphorylation by inleracting CIPKs, N-myristoylation and S-acylation with C16 and C18 fatty acids, S053 phosphorylation by 50S2 is thought to improve the stability of the SOS2-5053 protein kinase complex. N-myristoylation and S-aeylation determine S053 localization. membrane binding, and are essential for prote in function in planta. In the yeast system, howewer, S-acylation is dispensable for activalion 01 S051 . Moreover, a N-terminal poly-Iysine domain that is unique lo SOS3 mediates the binding to SOS1 and facilitates SOS3 tethering to the plasma membrane.
DescriptionComunicación oral presentada en the 2º International Meeting FOR1061: Plant Primary Metabolism: Synthesis, Storage and Degradation Processes in Heidelberg 7-9 mayo 2014 (Germany)
URIhttp://hdl.handle.net/10261/122336
Appears in Collections:(IRNAS) Comunicaciones congresos
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