scholarly journals Spatial regulation of the KH domain RNA-binding protein Rnc1 mediated by a Crm1-independent nuclear export system in Schizosaccharomyces pombe

2017 ◽  
Vol 104 (3) ◽  
pp. 428-448 ◽  
Author(s):  
Ryosuke Satoh ◽  
Yasuhiro Matsumura ◽  
Akitomo Tanaka ◽  
Makoto Takada ◽  
Yuna Ito ◽  
...  
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Nuclear Export ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Spatial Regulation ◽  
Kh Domain ◽  
Export System

scholarly journals The RNA-binding protein Sam68 is a multifunctional player in human cancer

2011 ◽  
Vol 18 (4) ◽  
pp. R91-R102 ◽  
Author(s):  
Pamela Bielli ◽  
Roberta Busà ◽  
Maria Paola Paronetto ◽  
Claudio Sette
Keyword(s):  
Nuclear Export ◽  
Rna Binding ◽  
Viral Infections ◽  
Human Cancer ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Mrna Translation ◽  
Endocrine Tumors ◽  
Recent Advancement ◽  
Kh Domain

Src associated in mitosis, of 68 kDa (Sam68) is a KH domain RNA-binding protein that belongs to the signal transduction and activation of RNA family. Although ubiquitously expressed, Sam68 plays very specialized roles in different cellular environments. In most cells, Sam68 resides in the nucleus and is involved in several steps of mRNA processing, from transcription, to alternative splicing, to nuclear export. In addition, Sam68 translocates to the cytoplasm upon cell stimulation, cell cycle transitions or viral infections, where it takes part to signaling complexes and associates with the mRNA translation machinery. Recent evidence has linked Sam68 function to the onset and progression of endocrine tumors, such as prostate and breast carcinomas. Notably, all the biochemical activities reported for Sam68 seem to be implicated in carcinogenesis. Herein, we review the recent advancement in the knowledge of Sam68 function and regulation and discuss it in the frame of its participation to neoplastic transformation and tumor progression.

scholarly journals The Arabidopsis KH-Domain RNA-Binding Protein ESR1 Functions in Components of Jasmonate Signalling, Unlinking Growth Restraint and Resistance to Stress

PLoS ONE ◽  
2015 ◽  
Vol 10 (5) ◽  
pp. e0126978 ◽  
Author(s):  
Louise F. Thatcher ◽  
Lars G. Kamphuis ◽  
James K. Hane ◽  
Luis Oñate-Sánchez ◽  
Karam B. Singh
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Kh Domain ◽  
Resistance To Stress ◽  
Jasmonate Signalling

scholarly journals The RNA-binding protein FMRP facilitates the nuclear export of N6-methyladenosine–containing mRNAs

2019 ◽  
Vol 294 (52) ◽  
pp. 19889-19895 ◽  
Author(s):  
Phillip J. Hsu ◽  
Hailing Shi ◽  
Allen C. Zhu ◽  
Zhike Lu ◽  
Nimrod Miller ◽  
...  
Keyword(s):  
Nuclear Export ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein

scholarly journals The RNA Binding Protein Csx1 Promotes Sexual Differentiation in Schizosaccharomyces pombe

PLoS ONE ◽  
2012 ◽  
Vol 7 (1) ◽  
pp. e30067 ◽  
Author(s):  
Ana M. Matia-Gonzalez ◽  
Jael Sotelo ◽  
Miguel A. Rodriguez-Gabriel
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Sexual Differentiation ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein

scholarly journals The RNA-binding protein Staufen1 is increased in DM1 skeletal muscle and promotes alternative pre-mRNA splicing

2012 ◽  
Vol 196 (6) ◽  
pp. 699-712 ◽  
Author(s):  
Aymeric Ravel-Chapuis ◽  
Guy Bélanger ◽  
Ramesh S. Yadava ◽  
Mani S. Mahadevan ◽  
Luc DesGroseillers ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Alternative Splicing ◽  
Nuclear Export ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Splicing Regulation ◽  
Ribonucleic Acids ◽  
Dystrophia Myotonica Protein Kinase

In myotonic dystrophy type 1 (DM1), dystrophia myotonica protein kinase messenger ribonucleic acids (RNAs; mRNAs) with expanded CUG repeats (CUGexp) aggregate in the nucleus and become toxic to cells by sequestering and/or misregulating RNA-binding proteins, resulting in aberrant alternative splicing. In this paper, we find that the RNA-binding protein Staufen1 is markedly and specifically increased in skeletal muscle from DM1 mouse models and patients. We show that Staufen1 interacts with mutant CUGexp mRNAs and promotes their nuclear export and translation. This effect is critically dependent on the third double-stranded RNA–binding domain of Staufen1 and shuttling of Staufen1 into the nucleus via its nuclear localization signal. Moreover, we uncover a new role of Staufen1 in splicing regulation. Overexpression of Staufen1 rescues alternative splicing of two key pre-mRNAs known to be aberrantly spliced in DM1, suggesting its increased expression represents an adaptive response to the pathology. Altogether, our results unravel a novel function for Staufen1 in splicing regulation and indicate that it may positively modulate the complex DM1 phenotype, thereby revealing its potential as a therapeutic target.

scholarly journals A KH-Domain RNA-Binding Protein Interacts with FIERY2/CTD Phosphatase-Like 1 and Splicing Factors and Is Important for Pre-mRNA Splicing in Arabidopsis

PLoS Genetics ◽  
2013 ◽  
Vol 9 (10) ◽  
pp. e1003875 ◽  
Author(s):  
Tao Chen ◽  
Peng Cui ◽  
Hao Chen ◽  
Shahjahan Ali ◽  
Shoudong Zhang ◽  
...  
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Mrna Splicing ◽  
Splicing Factors ◽  
Kh Domain ◽  
Ctd Phosphatase

scholarly journals Phosphorylation and nuclear transit modulate the balance between normal function and terminal aggregation of the yeast RNA-binding protein Ssd1

2017 ◽  
Vol 28 (22) ◽  
pp. 3057-3069 ◽  
Author(s):  
Cornelia Kurischko ◽  
James R. Broach
Keyword(s):  
Rna Polymerase Ii ◽  
Nuclear Export ◽  
Rna Binding ◽  
Binding Protein ◽  
Neurological Diseases ◽  
Rna Binding Protein ◽  
Normal Function ◽  
Nuclear Localization Sequence ◽  
P Bodies ◽  
Localization Sequence

Yeast Ssd1 is an RNA-binding protein that shuttles between the nucleus and cytoplasm. Ssd1 interacts with its target mRNAs initially during transcription by binding through its N-terminal prion-like domain (PLD) to the C-terminal domain of RNA polymerase II. Ssd1 subsequently targets mRNAs acquired in the nucleus either to daughter cells for translation or to stress granules (SGs) and P-bodies (PBs) for mRNA storage or decay. Here we show that PB components assist in the nuclear export of Ssd1and subsequent targeting of Ssd1 to PB sites in the cytoplasm. In the absence of import into the nucleus, Ssd1 fails to associate with PBs in the cytoplasm but rather is targeted to cytosolic insoluble protein deposits (IPODs). The association of Ssd1 either with IPOD sites or with PB/SG requires the PLD, whose activity is differentially regulated by the Ndr/LATS family kinase, Cbk1: phosphorylation suppresses PB/SG association but enhances IPOD formation. This regulation likely accrues from a phosphorylation-sensitive nuclear localization sequence located in the PLD. The results presented here may inform our understanding of aggregate formation by RBP in certain neurological diseases.

scholarly journals The RNA-Binding Protein SBR (Dm NXF1) Is Required for the Constitution of Medulla Boundaries in Drosophila melanogaster Optic Lobes

Cells ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 1144
Author(s):  
Ludmila Mamon ◽  
Anna Yakimova ◽  
Daria Kopytova ◽  
Elena Golubkova
Keyword(s):  
Drosophila Melanogaster ◽  
Glial Cells ◽  
Nuclear Export ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Cytoplasmic Localization ◽  
Optic Lobes ◽  
Axon Bundle

Drosophila melanogaster sbr (small bristles) is an orthologue of the Nxf1 (nuclear export factor 1) genes in different Opisthokonta. The known function of Nxf1 genes is the export of various mRNAs from the nucleus to the cytoplasm. The cytoplasmic localization of the SBR protein indicates that the nuclear export function is not the only function of this gene in Drosophila. RNA-binding protein SBR enriches the nucleus and cytoplasm of specific neurons and glial cells. In sbr12 mutant males, the disturbance of medulla boundaries correlates with the defects of photoreceptor axons pathfinding, axon bundle individualization, and developmental neurodegeneration. RNA-binding protein SBR participates in processes allowing axons to reach and identify their targets.

Sign in / Sign up

Export Citation Format

Share Document