scholarly journals The RNA Binding Protein ELF9 Directly Reduces SUPPRESSOR OF OVEREXPRESSION OF CO1 Transcript Levels in Arabidopsis, Possibly via Nonsense-Mediated mRNA Decay

2009 ◽  
Vol 21 (4) ◽  
pp. 1195-1211 ◽  
Author(s):  
Hae-Ryong Song ◽  
Ju-Dong Song ◽  
Jung-Nam Cho ◽  
Richard M. Amasino ◽  
Bosl Noh ◽  
...  
Keyword(s):  
Mrna Decay ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Transcript Levels ◽  
Nonsense Mediated Mrna Decay

scholarly journals Activation and inhibition of nonsense-mediated mRNA decay control the abundance of alternative polyadenylation products

2020 ◽  
Author(s):  
Aparna Kishor ◽  
Sarah E Fritz ◽  
Nazmul Haque ◽  
Zhiyun Ge ◽  
Ilker Tunc ◽  
...  
Keyword(s):  
Mrna Decay ◽  
Rna Binding ◽  
Rna Binding Protein ◽  
Alternative Polyadenylation ◽  
Transcript Level ◽  
Untranslated Regions ◽  
Multiple Tumor ◽  
The Core ◽  
Nonsense Mediated Mrna Decay ◽  
Tumor Types

Abstract Alternative polyadenylation (APA) produces transcript 3′ untranslated regions (3′UTRs) with distinct sequences, lengths, stabilities and functions. We show here that APA products include a class of cryptic nonsense-mediated mRNA decay (NMD) substrates with extended 3′UTRs that gene- or transcript-level analyses of NMD often fail to detect. Transcriptome-wide, the core NMD factor UPF1 preferentially recognizes long 3′UTR products of APA, leading to their systematic downregulation. Counteracting this mechanism, the multifunctional RNA-binding protein PTBP1 regulates the balance of short and long 3′UTR isoforms by inhibiting NMD, in addition to its previously described modulation of co-transcriptional polyadenylation (polyA) site choice. Further, we find that many transcripts with altered APA isoform abundance across multiple tumor types are controlled by NMD. Together, our findings reveal a widespread role for NMD in shaping the outcomes of APA.

scholarly journals Picornavirus Modification of a Host mRNA Decay Protein

mBio ◽  
2012 ◽  
Vol 3 (6) ◽  
Author(s):  
Janet M. Rozovics ◽  
Amanda J. Chase ◽  
Andrea L. Cathcart ◽  
Wayne Chou ◽  
Paul D. Gershon ◽  
...  
Keyword(s):  
Host Cell ◽  
Mrna Decay ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Rna Replication ◽  
Human Rhinovirus ◽  
Genomic Rnas

ABSTRACTDue to the limited coding capacity of picornavirus genomic RNAs, host RNA binding proteins play essential roles during viral translation and RNA replication. Here we describe experiments suggesting that AUF1, a host RNA binding protein involved in mRNA decay, plays a role in the infectious cycle of picornaviruses such as poliovirus and human rhinovirus. We observed cleavage of AUF1 during poliovirus or human rhinovirus infection, as well as interaction of this protein with the 5′ noncoding regions of these viral genomes. Additionally, the picornavirus proteinase 3CD, encoded by poliovirus or human rhinovirus genomic RNAs, was shown to cleave all four isoforms of recombinant AUF1 at a specific N-terminal sitein vitro. Finally, endogenous AUF1 was found to relocalize from the nucleus to the cytoplasm in poliovirus-infected HeLa cells to sites adjacent to (but distinct from) putative viral RNA replication complexes.IMPORTANCEThis study derives its significance from reporting how picornaviruses like poliovirus and human rhinovirus proteolytically cleave a key player (AUF1) in host mRNA decay pathways during viral infection. Beyond cleavage of AUF1 by the major viral proteinase encoded in picornavirus genomes, infection by poliovirus results in the relocalization of this host cell RNA binding protein from the nucleus to the cytoplasm. The alteration of both the physical state of AUF1 and its cellular location illuminates how small RNA viruses manipulate the activities of host cell RNA binding proteins to ensure a faithful intracellular replication cycle.

scholarly journals Fragile X-Related Protein 1 (FXR1) Promotes Trophoblast Migration at Early Pregnancy via Downregulation of GDF-15 Expression

2021 ◽  
Author(s):  
Wei Hong ◽  
Jin-Hong Chen ◽  
Hong-jiao Ma ◽  
Li-Li ◽  
Xiao-Cui Li
Keyword(s):  
Mrna Decay ◽  
Rna Binding ◽  
Ex Vivo ◽  
Fragile X ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Explant Culture ◽  
Extravillous Trophoblast ◽  
Related Protein ◽  
Trophoblast Migration

AbstractFragile X-related protein 1 (FXR1) is an RNA-binding protein that can regulate specific mRNA decay in cells. Our previous study showed that FXR1 expression was significantly decreased in trophoblasts from patients with unexplained recurrent spontaneous abortion (RSA); however, the role of FXR1 in trophoblast function during early placenta development has not been fully elucidated. In this study, we found that knockdown of FXR1 using siRNA effectively inhibited the migration of HTR-8 cells and extravillous trophoblast (EVT) outgrowth in an ex vivo extravillous explant culture model. Furthermore, through analysis of a panel of cytokines, we found that the GDF-15 protein was upregulated after knockdown of FXR1 in HTR-8/SVneo cells. This was further confirmed by western blotting and immunofluorescence in HTR-8/SVneo cells and an extravillous explant. Our data also showed that FXR1 expression was downregulated and GDF-15 was upregulated in chorionic villous tissues from RSA patients compared with those from healthy controls (HCs). Further, immunohistochemistry showed a strong expression of GDF-15 in chorionic villous tissue in the RSA group, which was mainly distributed in villous trophoblasts (CTBs) and syncytiotrophoblasts (STBs). Moreover, knockdown of GDF-15 enhanced the migration of HTR-8 cells, while overexpression of GDF-15 using plasmid or treatment with recombinant human GDF-15 protein inhibited trophoblast migration. Importantly, RNA-binding protein immunoprecipitation showed that FXR1 directly bound to the 3′-UTR of GDF-15 mRNA to promote GDF-15 mRNA decay. Together, our data provide new insight into the function of FXR1 in human placenta via regulation of GDF-15 expression in trophoblasts and suggest a possible pathological process involved in RSA.

scholarly journals Role for Upf2p Phosphorylation in Saccharomyces cerevisiae Nonsense-Mediated mRNA Decay

2006 ◽  
Vol 26 (9) ◽  
pp. 3390-3400 ◽  
Author(s):  
Weirong Wang ◽  
Iván J. Cajigas ◽  
Stuart W. Peltz ◽  
Miles F. Wilkinson ◽  
Carlos I. González
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Mrna Decay ◽  
Rna Binding ◽  
Rna Binding Protein ◽  
Nonsense Mediated Mrna Decay ◽  
Higher Eukaryotes ◽  
Nonsense Codons ◽  
First Time

ABSTRACT Premature termination (nonsense) codons trigger rapid mRNA decay by the nonsense-mediated mRNA decay (NMD) pathway. Two conserved proteins essential for NMD, UPF1 and UPF2, are phosphorylated in higher eukaryotes. The phosphorylation and dephosphorylation of UPF1 appear to be crucial for NMD, as blockade of either event in Caenorhabditis elegans and mammals largely prevents NMD. The universality of this phosphorylation/dephosphorylation cycle pathway has been questioned, however, because the well-studied Saccharomyces cerevisiae NMD pathway has not been shown to be regulated by phosphorylation. Here, we used in vitro and in vivo biochemical techniques to show that both S. cerevisiae Upf1p and Upf2p are phosphoproteins. We provide evidence that the phosphorylation of the N-terminal region of Upf2p is crucial for its interaction with Hrp1p, an RNA-binding protein that we previously showed is essential for NMD. We identify specific amino acids in Upf2p's N-terminal domain, including phosphorylated serines, which dictate both its interaction with Hrp1p and its ability to elicit NMD. Our results indicate that phosphorylation of UPF1 and UPF2 is a conserved event in eukaryotes and for the first time provide evidence that Upf2p phosphorylation is crucial for NMD.

scholarly journals Staufen1 and UPF1 exert opposite actions on the replacement of the nuclear cap-binding complex by eIF4E at the 5′ end of mRNAs

2019 ◽  
Vol 47 (17) ◽  
pp. 9313-9328 ◽  
Author(s):  
Kwon Jeong ◽  
Incheol Ryu ◽  
Joori Park ◽  
Hyun Jung Hwang ◽  
Hongseok Ha ◽  
...  
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Functional Importance ◽  
Double Stranded Rna ◽  
Importin Α ◽  
Cap Binding Complex ◽  
Nonsense Mediated Mrna Decay ◽  
Cellular Apoptosis ◽  
Transcriptional Gene Regulation

Abstract Newly synthesized mRNAs are exported from the nucleus to cytoplasm with a 5′-cap structure bound by the nuclear cap-binding complex (CBC). During or after export, the CBC should be properly replaced by cytoplasmic cap-binding protein eIF4E for efficient protein synthesis. Nonetheless, little is known about how the replacement takes place. Here, we show that double-stranded RNA-binding protein staufen1 (STAU1) promotes efficient replacement by facilitating an association between the CBC–importin α complex and importin β. Our transcriptome-wide analyses and artificial tethering experiments also reveal that the replacement occurs more efficiently when an mRNA associates with STAU1. This event is inhibited by a key nonsense-mediated mRNA decay factor, UPF1, which directly interacts with STAU1. Furthermore, we find that cellular apoptosis that is induced by ionizing radiation is accompanied by inhibition of the replacement via increased association between STAU1 and hyperphosphorylated UPF1. Altogether, our data highlight the functional importance of STAU1 and UPF1 in the course of the replacement of the CBC by eIF4E, adding a previously unappreciated layer of post-transcriptional gene regulation.

scholarly journals Targeted mRNA Decay by RNA Binding Protein AUF1 Regulates Adult Muscle Stem Cell Fate, Promoting Skeletal Muscle Integrity

Cell Reports ◽  
2016 ◽  
Vol 16 (5) ◽  
pp. 1379-1390 ◽  
Author(s):  
Devon M. Chenette ◽  
Adam B. Cadwallader ◽  
Tiffany L. Antwine ◽  
Lauren C. Larkin ◽  
Jinhua Wang ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Stem Cell ◽  
Cell Fate ◽  
Mrna Decay ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Muscle Stem Cell ◽  
Stem Cell Fate ◽  
Adult Muscle

235: The RNA-Binding Protein IMP3: A Novel Molecular Marker Predicts Progression of Superficial (TA and T1) Urothelial Carcinomas of Bladder

2007 ◽  
Vol 177 (4S) ◽  
pp. 78-79
Author(s):  
Lioudmila Sitnikova ◽  
Gary Mendese ◽  
Qin Lui ◽  
Bruce A. Woda ◽  
Di Lu ◽  
...  
Keyword(s):  
Molecular Marker ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Urothelial Carcinomas
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