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Nucleo-cytoplasmic distribution of SAP18 reveals its dual function in splicing regulation and heat stress responses in Arabidopsis

ABSTRACT: RNA-seq experiment of Col0, sr45, and sap18 mutants

ORGANISM(S): Arabidopsis thaliana

PROVIDER: GSE280686 | GEO | 2024/10/31

REPOSITORIES: GEO

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Nucleo-cytoplasmic distribution of SAP18 reveals its dual function in splicing regulation and heat stress response in Arabidopsis

Project description:RNA-seq experiment of Col0, sr45, sap18sr45 and asap (sap18sr45acinus) mutants

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Nucleo-cytoplasmic distribution of SAP18 reveals its dual function in splicing and thermotolerance in Arabidopsis

Project description:The dynamic shuttling of proteins between the nucleus and cytoplasm orchestrates vital functions in eukaryotes. Here, we unveil multifaceted functions of Arabidopsis Sin3-associated protein 18 kDa (SAP18) in regulating development and stress tolerance. As a crucial component of the Apoptosis- and Splicing-Associated Protein (ASAP) complex in the nucleus, SAP18 plays an integral role in the precise splicing of genes associated with leaf development, decoding its significance in post-transcriptional regulatory networks. Under heat shock conditions, SAP18 relocates to cytoplasmic stress granules and processing bodies, suggesting a novel thermoprotective role. This dual localization highlights SAP18 versatility in coordinating cellular responses, encompassing both nuclear splicing regulation and cytoplasmic stress granule dynamics. Our findings significantly expand the understanding of the intricate involvement of SAP18 in plant growth, and pave the way for future exploration of its diverse functions in thermotolerance mechanisms.

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Nucleo-cytoplasmic distribution of SAP18 reveals its dual function in splicing regulation and heat stress responses in Arabidopsis

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Nucleo-cytoplasmic distribution of SAP18 reveals its dual function in splicing regulation and heat stress response in Arabidopsis

Project description:Nucleo-cytoplasmic distribution of SAP18 reveals its dual function in splicing regulation and heat stress response in Arabidopsis

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Nucleo-cytoplasmic Partitioning of ARF Proteins Controls Auxin Responses in Arabidopsis thaliana.

Project description:The phytohormone auxin plays crucial roles in nearly every aspect of plant growth and development. The auxin response factor (ARF) transcription factor family regulates auxin-responsive gene expression and exhibits nuclear localization in regions of high auxin responsiveness. Here we show that the ARF7 and ARF19 proteins accumulate in micron-sized assemblies within the cytoplasm of tissues with attenuated auxin responsiveness. We found that the intrinsically disordered middle region and the folded PB1 interaction domain of ARFs drive protein assembly formation. Mutation of a single lysine within the PB1 domain abrogates cytoplasmic assemblies, promotes ARF nuclear localization, and results in an altered transcriptome and morphological defects. Our data suggest a model in which ARF nucleo-cytoplasmic partitioning regulates auxin responsiveness, providing a mechanism for cellular competence for auxin signaling.

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Nucleo-cytoplasmic shuttling of splicing factor SRSF1 is required for development and cilia function.

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Project description:The metazoan protein BCL2-associated athanogene cochaperone 6 (Bag6) forms a hetero-trimeric complex with ubiquitin-like 4A and transmembrane domain recognition complex 35 (TRC35). This Bag6 complex is involved in tail-anchored protein targeting and various protein quality-control pathways in the cytosol as well as regulating transcription and histone methylation in the nucleus. Here we present a crystal structure of Bag6 and its cytoplasmic retention factor TRC35, revealing that TRC35 is remarkably conserved throughout the opisthokont lineage except at the C-terminal Bag6-binding groove, which evolved to accommodate Bag6, a unique metazoan factor. While TRC35 and its fungal homolog, guided entry of tail-anchored protein 4 (Get4), utilize a conserved hydrophobic patch to bind their respective partners, Bag6 wraps around TRC35 on the opposite face relative to the Get4-5 interface. We further demonstrate that TRC35 binding is critical not only for occluding the Bag6 nuclear localization sequence from karyopherin ? to retain Bag6 in the cytosol but also for preventing TRC35 from succumbing to RNF126-mediated ubiquitylation and degradation. The results provide a mechanism for regulation of Bag6 nuclear localization and the functional integrity of the Bag6 complex in the cytosol.

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