ArticlePloS one2008
Analyses of in vivo interaction and mobility of two spliceosomal proteins using FRAP and BiFC.
Article in PloS one, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 36 citations in OpenAlex.
- Alternative splicing regulation in plants by SP7-like effectors from symbiotic arbuscular mycorrhizal fungi.Nature communications · 2024Article
- Alternative Splicing Variation: Accessing and Exploiting in Crop Improvement Programs.International journal of molecular sciences · 2023Review
- MDF is a conserved splicing factor and modulates cell division and stress response inLife science alliance · 2023Article
- The Arabidopsis splicing regulator SR45 confers salt tolerance in a splice isoform-dependent manner.Plant molecular biology · 2019Article
- RiCRN1, a Crinkler Effector From the Arbuscular Mycorrhizal FungusFrontiers in microbiology · 2018Article
- The Arabidopsis SR45 Splicing Factor, a Negative Regulator of Sugar Signaling, Modulates SNF1-Related Protein Kinase 1 Stability.The Plant cell · 2016Article
- Transcriptome-Wide Identification of RNA Targets of Arabidopsis SERINE/ARGININE-RICH45 Uncovers the Unexpected Roles of This RNA Binding Protein in RNA Processing.The Plant cell · 2015Article
- Phosphothreonine 218 is required for the function of SR45.1 in regulating flower petal development in Arabidopsis.Plant signaling & behavior · 2014Article
- On the physiological significance of alternative splicing events in higher plants.Protoplasma · 2013Review
- Article
- The quest for four-dimensional imaging in plant cell biology: it's just a matter of time.Annals of botany · 2012Review
- Localization and dynamics of nuclear speckles in plants.Plant physiology · 2012Review
- The differential interaction of snRNPs with pre-mRNA reveals splicing kinetics in living cells.The Journal of cell biology · 2010Article
- The plant-specific SR45 protein negatively regulates glucose and ABA signaling during early seedling development in Arabidopsis.Plant physiology · 2010Article
- Calcium/calmodulin-regulated receptor-like kinase CRLK1 interacts with MEKK1 in plants.Plant signaling & behavior · 2010Article
- Dynamic nucleocytoplasmic shuttling of an Arabidopsis SR splicing factor: role of the RNA-binding domains.Plant physiology · 2010Article
- Two alternatively spliced isoforms of the Arabidopsis SR45 protein have distinct roles during normal plant development.Plant physiology · 2009Article
- Plant-specific SR-related protein atSR45a interacts with spliceosomal proteins in plant nucleus.Plant molecular biology · 2009Article
- Article
- The dynamic pathway of nuclear RNA in eukaryotes.Nucleus (Austin, Tex.)Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
U1-70K, a U1 snRNP-specific protein, and serine/arginine-rich (SR) proteins are components of the spliceosome and play critical roles in both constitutive and alternative pre-mRNA splicing. However, the mobility properties of U1-70K, its in vivo interaction with SR proteins, and the mobility of the U1-70K-SR protein complex have not been studied in any system. Here, we studied the in vivo interaction of U1-70K with an SR protein (SR45) and the mobility of the U1-70K/SR protein complex using bimolecular fluorescence complementation (BiFC) and fluorescence recovery after photobleaching (FRAP). Our results show that U1-70K exchanges between speckles and the nucleoplasmic pool very rapidly and that this exchange is sensitive to ongoing transcription and phosphorylation. BiFC analyses showed that U1-70K and SR45 interacted primarily in speckles and that this interaction is mediated by the RS1 or RS2 domain of SR45. FRAP analyses showed considerably slower recovery of the SR45/U1-70K complex than either protein alone indicating that SR45/U1-70K complexes remain in the speckles for a longer duration. Furthermore, FRAP analyses with SR45/U1-70K complex in the presence of inhibitors of phosphorylation did not reveal any significant change compared to control cells, suggesting that the mobility of the complex is not affected by the status of protein phosphorylation. These results indicate that U1-70K, like SR splicing factors, moves rapidly in the nucleus ensuring its availability at various sites of splicing. Furthermore, although it appears that U1-70K moves by diffusion its mobility is regulated by phosphorylation and transcription.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.