Domains involved in TAF15 subcellular localisation: Dependence on cell type and ongoing transcription

Marko, Marija; Vlassis, Arsenios; Guialis, Apostolia; Leichter, Michael

doi:10.1016/j.gene.2012.06.088

Cited by 37 publications

(29 citation statements)

References 44 publications

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“…We also analyzed the subcellular distribution of TAF15b in stable transgenic plants expressing CsVp :: TAF15b‐GFP . TAF15b was mainly located in the nuclei and formed nucleoplasmic foci but it was excluded from the nucleoli, similar to the distribution pattern of human FUS and TAF15 (Figure c, d) (Marko et al ., ; Yang et al ., ). Dong et al .…”

Section: Resultsmentioning

confidence: 99%

TAF15b, involved in the autonomous pathway for flowering, represses transcription of FLOWERING LOCUS C

et al. 2017

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SUMMARYTATA-binding protein-associated factors (TAFs) are general transcription factors within the transcription factor IID (TFIID) complex, which recognizes the core promoter of genes. In addition to their biochemical function, it is known that several TAFs are involved in the regulation of developmental processes. In this study, we found that TAF15b affects flowering time, especially through the autonomous pathway (AP) in Arabidopsis. The mutant taf15b shows late flowering compared with the wild type plant during both long and short days, and vernalization accelerates the flowering time of taf15b. In addition, taf15b shows strong upregulation of FLOWERING LOCUS C (FLC), a flowering repressor in Arabidopsis, and the flc taf15b double mutant completely offsets the late flowering of taf15b, indicating that TAF15b is a typical AP gene. The taf15b mutant also shows increased transcript levels of COOLAIR, an antisense transcript of FLC. Consistently, chromatin immunoprecipitation (ChIP) analyses showed that the TAF15b protein is enriched around both sense and antisense transcription start sites of the FLC locus. In addition, co-immunoprecipitation showed that TAF15b interacts with RNA polymerase II (Pol II), while ChIP showed increased enrichment of the phosphorylated forms, both serine 2 (Ser2) and Ser5, of the C-terminal domain of Pol II at the FLC locus, which is indicative of transcriptional elongation. Finally, taf15b showed higher enrichment of the active histone marker, H3K4me3, on FLC chromatin. Taken together, our results suggest that TAF15b affects flowering time through transcriptional repression of FLC in Arabidopsis.

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Section: Resultsmentioning

confidence: 99%

TAF15b, involved in the autonomous pathway for flowering, represses transcription of FLOWERING LOCUS C

et al. 2017

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“…8A). It has been previously demonstrated that endogenous FUS and other FET family members undergo a partial shift to cytoplasm following inhibition of transcription (37,38). To assess effects of transcriptional arrest on FUS variants bearing a mutation in NLS but retaining nuclear localization, we treated cells expressing wild-type, R518K or R524T variants of FUS with actinomycin D. After 2 h in the majority of cells expressing either mutant, a significant portion of the protein was shifted to the cytoplasm (Fig.…”

Section: Resultsmentioning

confidence: 99%

Multistep process of FUS aggregation in the cell cytoplasm involves RNA-dependent and RNA-independent mechanisms

Shelkovnikova

Robinson

Southcombe

et al. 2014

Human Molecular Genetics

105

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Fused in sarcoma (FUS) is an RNA-binding protein involved in pathogenesis of several neurodegenerative diseases. Aggregation of mislocalized FUS into non-amyloid inclusions is believed to be pivotal in the development of cell dysfunction, but the mechanism of their formation is unclear. Using transient expression of a panel of deletion and chimeric FUS variants in various cultured cells, we demonstrated that FUS accumulating in the cytoplasm nucleates a novel type of RNA granules, FUS granules (FGs), that are structurally similar but not identical to physiological RNA transport granules. Formation of FGs requires FUS N-terminal prion-like domain and the ability to bind specific RNAs. Clustering of FGs coupled with further recruitment of RNA and proteins produce larger structures, FUS aggregates (FAs), that resemble but are clearly distinct from stress granules. In conditions of attenuated transcription, FAs lose RNA and dissociate into RNA-free FUS complexes that become precursors of large aggresome-like structures. We propose a model of multistep FUS aggregation involving RNA-dependent and RNA-independent stages. This model can be extrapolated to formation of pathological inclusions in human FUSopathies.

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“…Like FUS (Figure 3), EWSR1 and TAF15 each have an N-terminal PrLD, a glycine-rich region, and a single RRM, with C-terminal RGG-rich regions, a zinc-finger domain, and a PY-NLS [31,48,98,136,196,245–247]. Mutations shown were identified in ALS patients and compiled from Cady et al [228], Couthouis et al [48], Couthouis et al [98], Couthouis et al [136], Ticozzi et al [100], and the ALS Data Browser (http://alsdb.org) [135].…”

Section: Figurementioning

confidence: 99%

RNA-binding proteins with prion-like domains in health and disease

Harrison

Shorter

2017

Biochemical Journal

356

424

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Approximately 70 human RNA-binding proteins (RBPs) contain a prion-like domain (PrLD). PrLDs are low-complexity domains that possess a similar amino acid composition to prion domains in yeast, which enable several proteins, including Sup35 and Rnq1, to form infectious conformers, termed prions. In humans, PrLDs contribute to RBP function and enable RBPs to undergo liquid–liquid phase transitions that underlie the biogenesis of various membraneless organelles. However, this activity appears to render RBPs prone to misfolding and aggregation connected to neurodegenerative disease. Indeed, numerous RBPs with PrLDs, including TDP-43 (transactivation response element DNA-binding protein 43), FUS (fused in sarcoma), TAF15 (TATA-binding protein-associated factor 15), EWSR1 (Ewing sarcoma breakpoint region 1), and heterogeneous nuclear ribo-nucleoproteins A1 and A2 (hnRNPA1 and hnRNPA2), have now been connected via pathology and genetics to the etiology of several neurodegenerative diseases, including amyotrophic lateral sclerosis, frontotemporal dementia, and multisystem proteinopathy. Here, we review the physiological and pathological roles of the most prominent RBPs with PrLDs. We also highlight the potential of protein disaggregases, including Hsp104, as a therapeutic strategy to combat the aberrant phase transitions of RBPs with PrLDs that likely underpin neurodegeneration.

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Domains involved in TAF15 subcellular localisation: Dependence on cell type and ongoing transcription

Cited by 37 publications

References 44 publications

TAF15b, involved in the autonomous pathway for flowering, represses transcription of FLOWERING LOCUS C

TAF15b, involved in the autonomous pathway for flowering, represses transcription of FLOWERING LOCUS C

Multistep process of FUS aggregation in the cell cytoplasm involves RNA-dependent and RNA-independent mechanisms

RNA-binding proteins with prion-like domains in health and disease

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