Proteomic identification of a PSF/p54nrb heterodimer as RNF43 oncoprotein‐interacting proteins

Miyamoto, Kentaro; Sakurai, Hidetaka; Sugiura, Takeyuki

doi:10.1002/pmic.200800083

Cited by 14 publications

(14 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…To investigate how NONO/PSF might facilitate global pri-miRNA processing, we performed UV CrossLinking ImmunoPrecipitation coupled with deep sequencing (CLIP-seq) to identify their direct RNA targets. Both anti-NONO and anti-PSF antibodies efficiently brought down the NONO/PSF heterodimer, as reported earlier 40 , 41 , each of which was crosslinked to RNA, as detected by 32 p-labeling with T4 polynucleotide kinase ( Fig. 3a ; Supplementary Fig.…”

Section: Resultssupporting

confidence: 82%

NEAT1 scaffolds RNA-binding proteins and the Microprocessor to globally enhance pri-miRNA processing

Jiang

Shao

et al. 2017

Nat Struct Mol Biol

181

162

View full text Add to dashboard Cite

SummaryMicroRNA biogenesis is known to be modulated by a variety of RNA binding proteins (RBPs), but in most cases, individual RBPs appear to influence the processing of a small subset of target miRNAs. We herein report that the RNA binding NONO/PSF heterodimer binds a large number of expressed pri-miRNAs in HeLa cells to globally enhance pri-miRNA processing by the Drosha/DGCR8 Microprocessor. Because NONO/PSF are key components of paraspeckles organized by the lncRNA NEAT1, we further demonstrate that NEAT1 also has a profound effect on global pri-miRNA processing. Mechanistic dissection reveals that NEAT1 broadly interacts with NONO/PSF as well as many other RBPs, and that multiple RNA segments in NEAT1, including a “pseudo pri-miRNA” near its 3′ end, help attract the Microprocessor. These findings suggest a bird nest model for a large non-coding RNA to orchestrate efficient processing of almost an entire class of small non-coding RNAs in the nucleus.

show abstract

Section: Resultssupporting

confidence: 82%

NEAT1 scaffolds RNA-binding proteins and the Microprocessor to globally enhance pri-miRNA processing

Jiang

Shao

et al. 2017

Nat Struct Mol Biol

181

162

View full text Add to dashboard Cite

show abstract

“…Thus co-expressing the same SFPQ protein used for Crystal 1 along with the dimerization domain of NONO results in formation of SFPQ-276–598/NONO-53–312 heterodimers. We note that the SFPQ/NONO heterodimer may in fact be more physiologically relevant than the SFPQ homodimer, as SFPQ was first discovered as a heterodimer with NONO ( 33 ) and many studies since have observed SFPQ and NONO colocalized and co-purified ( 12 , 34 ).…”

Section: Resultsmentioning

confidence: 90%

The structure of human SFPQ reveals a coiled-coil mediated polymer essential for functional aggregation in gene regulation

Sadowska

Bekere

et al. 2015

Nucleic Acids Research

127

209

View full text Add to dashboard Cite

SFPQ, (a.k.a. PSF), is a human tumor suppressor protein that regulates many important functions in the cell nucleus including coordination of long non-coding RNA molecules into nuclear bodies. Here we describe the first crystal structures of Splicing Factor Proline and Glutamine Rich (SFPQ), revealing structural similarity to the related PSPC1/NONO heterodimer and a strikingly extended structure (over 265 Å long) formed by an unusual anti-parallel coiled-coil that results in an infinite linear polymer of SFPQ dimers within the crystals. Small-angle X-ray scattering and transmission electron microscopy experiments show that polymerization is reversible in solution and can be templated by DNA. We demonstrate that the ability to polymerize is essential for the cellular functions of SFPQ: disruptive mutation of the coiled-coil interaction motif results in SFPQ mislocalization, reduced formation of nuclear bodies, abrogated molecular interactions and deficient transcriptional regulation. The coiled-coil interaction motif thus provides a molecular explanation for the functional aggregation of SFPQ that directs its role in regulating many aspects of cellular nucleic acid metabolism.

show abstract

“…It has been shown to reside in the inner nuclear membrane, the nuclear periphery and nucleoplasm,10 the endoplasmic reticulum6 and on the surface cell membrane where it interacts with Frizzled 8. The presence of the signal peptide determines the distribution of RNF43 to the plasma membrane, while its lack results predominantly in the cytoplasmic dislocation 8…”

Section: Localisationmentioning

confidence: 99%

Rnf43

Serra

Chetty

2017

J Clin Pathol

View full text Add to dashboard Cite

RNF43 (E3 ubiquitin-protein ligase RNF43 or RING-type E3 ubiquitin transferase RNF43) functions as a tumor suppressor, by exerting a predominant negative feedback mechanism in the Wnt/β-catenin signaling pathway. RNF43 inhibits Wnt/beta-catenin signaling by ubiquitinating Frizzled receptor and targeting it to the lysosomal pathway for degradation. Loss of function of RNF43 results in decrease/lack of degradation of Frizzled with enhancement of Wnt/β-catenin signaling pathway. Mutations of RNF43 have been reported in different cancers. We describe the structure of RNF43, its function and most frequent mutations in different cancers.

show abstract

Proteomic identification of a PSF/p54nrb heterodimer as RNF43 oncoprotein‐interacting proteins

Cited by 14 publications

References 23 publications

NEAT1 scaffolds RNA-binding proteins and the Microprocessor to globally enhance pri-miRNA processing

NEAT1 scaffolds RNA-binding proteins and the Microprocessor to globally enhance pri-miRNA processing

The structure of human SFPQ reveals a coiled-coil mediated polymer essential for functional aggregation in gene regulation

Rnf43

Contact Info

Product

Resources

About