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See detailDynamic Distribution and Interaction of the Arabidopsis SRSF1 Subfamily Splicing Factors
Stankovic, Nancy ULg; Schloesser, Marie ULg; Joris, Marine ULg et al

in Plant Physiology (2016), 170

Serine/Arginine-rich (SR) proteins are essential nucleus-localized splicing factors. Our prior studies showed that Arabidopsis RSZ22, a homolog of the human SRSF7 SR factor, exits the nucleus through two ... [more ▼]

Serine/Arginine-rich (SR) proteins are essential nucleus-localized splicing factors. Our prior studies showed that Arabidopsis RSZ22, a homolog of the human SRSF7 SR factor, exits the nucleus through two pathways, either dependent or independent on the XPO1 receptor. Here, we examined the expression profiles and shuttling dynamics of the Arabidopsis SRSF1 subfamily (SR30, SR34, SR34a and SR34b) under control of their endogenous promoter in Arabidopsis and in transient expression assay. Due to its rapid nucleocytoplasmic shuttling and high expression level in transient assay, we analysed the multiple determinants that regulate the localisation and shuttling dynamics of SR34. By site-directed mutagenesis of SR34 RNA-binding sequences and RS domain, we further show that functional RRM1 or RRM2 are dispensable for the exclusive protein nuclear localization and speckle-like distribution. However, mutations of both RRMs induced aggregation of the protein whereas mutation in the RS domain decreased the stability of the protein and suppressed its nuclear accumulation. Furthermore, the RNA-binding motif mutants are defective for their export through the XPO1 (CRM1/Exportin-1) receptor pathway, but retain nucleocytoplasmic mobility. We performed a yeast two hybrid screen with SR34 as bait and discovered SR45 as a new interactor. SR45 is an unusual SR splicing factor bearing two RS domains. These interactions were confirmed in planta by FLIM-FRET and BiFC and the roles of SR34 domains in protein-protein interactions were further studied. Altogether, our report extends our understanding of shuttling dynamics of Arabidopsis SR splicing factors [less ▲]

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See detailFunctional study of Arabidopsis thaliana ASF/SF2-like pre-mRNA SR splicing factors
Stankovic, Nancy ULg; Tillemans, Vinciane; Leponce, Isabelle et al

Poster (2012, July 04)

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See detailRSZ22, a dynamic nucleocytoplasmic shuttling SR splicing factor
Tillemans, Vinciane ULg; Rausin, Glwadys; Stankovic, Nancy ULg et al

Poster (2011, March)

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See detailDynamic Nucleocytoplasmic Shuttling of an Arabidopsis SR Splicing Factor: Role of the RNA-Binding Domains
Rausin, Glwadys ULg; Tillemans, Vinciane ULg; Stankovic, Nancy ULg et al

in Plant Physiology (2010), 153

Serine/arginine-rich (SR) proteins are essential nuclear-localized splicing factors. We have investigated the dynamic subcellular distribution of the Arabidopsis (Arabidopsis thaliana) RSZp22 protein, a ... [more ▼]

Serine/arginine-rich (SR) proteins are essential nuclear-localized splicing factors. We have investigated the dynamic subcellular distribution of the Arabidopsis (Arabidopsis thaliana) RSZp22 protein, a homolog of the human 9G8 SR factor. Little is known about the determinants underlying the control of plant SR protein dynamics, and so far most studies relied on ectopic transient overexpression. Here, we provide a detailed analysis of the RSZp22 expression profile and describe its nucleocytoplasmic shuttling properties in specific cell types. Comparison of transient ectopic- and stable tissue-specific expression highlights the advantages of both approaches for nuclear protein dynamic studies. By site-directed mutagenesis of RSZp22 RNA-binding sequences, we show that functional RNA recognition motif RNP1 and zinc-knuckle are dispensable for the exclusive protein nuclear localization and speckle-like distribution. Fluorescence resonance energy transfer imaging also revealed that these motifs are implicated in RSZp22 molecular interactions. Furthermore, the RNA-binding motif mutants are defective for their export through the CRM1/XPO1/Exportin-1 receptor pathway but retain nucleocytoplasmic mobility. Moreover, our data suggest that CRM1 is a putative export receptor for mRNPs in plants. [less ▲]

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See detailFunctional study of Arabidopsis thaliana ASF/SF2-like pre-mRNA SR splicing factors
Stankovic, Nancy ULg; Tillemans, Vinciane; Hanikenne, Marc et al

Poster (2010, January 26)

Detailed reference viewed: 20 (7 ULg)