TFIP11, CCNL1 and EWSR1 Protein-protein Interactions, and Their Nuclear Localization

Tannukit, Sissada; Wen, Xin; Wang, Hongjun; Paine, Michael L.

doi:10.3390/ijms9081504

Cited by 14 publications

(10 citation statements)

References 26 publications

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“…AtNTR1 immunolocalisation was investigated, to test the relationship between AtNTR1 and PolII. We confirmed previous results from human cells showing that NTR1 is localised in the nucleus but excluded from the nucleolus, using a complementing genomic NTR1‐GFP line (Supplementary Fig S1I and J) and AtNTR1 antibody (Fig B) (Tannukit et al , ). In addition, it was found that AtNTR1 is only partially co‐localised with the SC35 splicing factor using dual labelling (Fig B), which is in agreement with results concerning NTR1 mouse homologue (Wen et al , ).…”

Section: Resultssupporting

confidence: 90%

NTR 1 is required for transcription elongation checkpoints at alternative exons in Arabidopsis

et al. 2015

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The interconnection between transcription and splicing is a subject of intense study. We report that Arabidopsis homologue of spliceosome disassembly factor NTR1 is required for correct expression and splicing of DOG1, a regulator of seed dormancy. Global splicing analysis in atntr1 mutants revealed a bias for downstream 5 0 and 3 0 splice site selection and an enhanced rate of exon skipping. A local reduction in PolII occupancy at misspliced exons and introns in atntr1 mutants suggests that directionality in splice site selection is a manifestation of fast PolII elongation kinetics. In agreement with this model, we found AtNTR1 to bind target genes and co-localise with PolII. A minigene analysis further confirmed that strong alternative splice sites constitute an AtNTR1-dependent transcriptional roadblock. Plants deficient in PolII endonucleolytic cleavage showed opposite effects for splice site choice and PolII occupancy compared to atntr1 mutants, and inhibition of PolII elongation or endonucleolytic cleavage in atntr1 mutant resulted in partial reversal of splicing defects. We propose that AtNTR1 is part of a transcription elongation checkpoint at alternative exons in Arabidopsis.

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Section: Resultssupporting

confidence: 90%

NTR 1 is required for transcription elongation checkpoints at alternative exons in Arabidopsis

et al. 2015

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“…To date no disease process has been identified for a mutated TFIP11 gene locus, but aberrant splicing activities are noted in many cancers [25,26], and the molecular mechanisms responsible may relate to key splicing factor activities being adversely impacted by specific mutations. Previously, we showed that TFIP11 interacts with cyclin L1 (CCNL1) and Ewing’s sarcoma protein (EWSR1), both of which have been previously associated with pre-mRNA splicing events [16]. It is intriguing that TFIP11 may participate in multiple cellular activities as diverse as pre-mRNA splicing, cell cycle activity and tumorigenesis.…”

Section: Discussionmentioning

confidence: 99%

“…Prior to imaging, cells were washed with phosphate buffered saline (PBS), fixed with 4% paraformaldehyde, counterstained with DAPI, mounted in VECTASHIELD medium (Vector Labs, Burlingame, CA). Direct fluorescence confocal microscopy was performed and images were captured as previously described [3,12,16]. …”

Section: Methodsmentioning

confidence: 99%

Identification of a novel nuclear localization signal and speckle-targeting sequence of tuftelin-interacting protein 11, a splicing factor involved in spliceosome disassembly

Tannukit

Crabb

Hertel

et al. 2009

Biochemical and Biophysical Research Communications

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Tuftelin-interacting protein 11 (TFIP11) is a protein component of the spliceosome complex that promotes the release of the lariat-intron during late-stage splicing through a direct recruitment and interaction with DHX15/PRP43. Expression of TFIP11 is essential for cell and organismal survival. TFIP11 contains a G-patch domain, a signature motif of RNA-processing proteins that is responsible for TFIP11-DHX15 interactions. No other functional domains within TFIP11 have been described. TFIP11 is localized to distinct speckled regions within the cell nucleus, although excluded from the nucleolus. In this study sequential C-terminal deletions and mutational analyses have identified two novel protein elements in mouse TFIP11. The first domain covers amino acids 701-706 (VKDKFN) and is an atypical nuclear localization signal (NLS). The second domain is contained within amino acids 711-735 and defines TFIP11's distinct speckled nuclear localization. The identification of a novel TFIP11 nuclear speckle targeting sequence (TFIP11-STS) suggests that this domain directly interacts with additional spliceosomal components. These data help define the mechanism of nuclear/ nuclear speckle localization of the splicing factor TFIP11, with implications for it's function.

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“…EWSR1 activates other transcription factors such as POU4F1 (or BRN3A, 13q13) [7], and POU5F1 (or OCT4, 6p21) genes which regulate differentiation of neuronal cells [7, 8]. EWSR1 and CCNL1 (cyclin L1) are also interacting partners of TFIP11 (tuftelin-interacting protein 11), a protein functionally related to the spliceosome and involved in pre-mRNA splicing [9]. In normal cell physiology, EWSR1 is required for cell survival in the central nervous system [4] and performs important functions in the regulation of genomic integrity and in RNA and microRNA’s maturation processes.…”

Section: Ews Protein In Normal Cell Physiologymentioning

confidence: 99%

Molecular detection and targeting of EWSR1 fusion transcripts in soft tissue tumors

et al. 2013

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Soft tissue tumors are a heterogeneous group of tumors, traditionally classified according to morphology and histogenesis. Molecular classification divides sarcomas into two main categories: (a) sarcomas with specific genetic alterations and (b) sarcomas showing multiple complex karyotypic abnormalities without any specific pattern. Most chromosomal alterations are represented by translocations which are increasingly detected. The identification of fusion transcripts, in fact, not only support the diagnosis but also provides the basis for the development of new therapeutic strategies aimed at blocking aberrant activity of the chimeric proteins. One of the genes most susceptible to breakage/translocation in soft tissue tumors is represented by Ewing sarcoma breakpoint region 1 (EWSR1). This gene has a large number of fusion partners, mainly associated with the pathogenesis of Ewing’s sarcoma but with other soft tissue tumors too. In this review, we illustrate the characteristics of this gene/protein, both in normal cellular physiology and in carcinogenesis. We describe the different fusion partners of EWSR1, the molecular pathways in which is involved and the main molecular biology techniques for the identification of fusion transcripts and for their inhibition.

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TFIP11, CCNL1 and EWSR1 Protein-protein Interactions, and Their Nuclear Localization

Cited by 14 publications

References 26 publications

NTR 1 is required for transcription elongation checkpoints at alternative exons in Arabidopsis

NTR 1 is required for transcription elongation checkpoints at alternative exons in Arabidopsis

Identification of a novel nuclear localization signal and speckle-targeting sequence of tuftelin-interacting protein 11, a splicing factor involved in spliceosome disassembly

Molecular detection and targeting of EWSR1 fusion transcripts in soft tissue tumors

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