<i>Drosophila</i> Brain Tumor is a translational repressor

Sonoda, Junichiro; Wharton, Robin P.

doi:10.1101/gad.870801

Cited by 295 publications

(338 citation statements)

References 52 publications

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“…Pum1 and Pum2 interact with different proteins that mediate their function as translational regulators. That is, Pum1-mediated translational repression of Hunchback mRNA requires an interaction with the zinc finger protein Nanos (NOS) and the NHL (NCL-1, HT2A, LIN-41) (Slack and Ruvkun 1998) domain protein Brain Tumor (BRAT) (Sonoda and Wharton 2001). In vitro, Pum1 interacts with the Nanos homolog XCat2; in Xenopus oocytes, it interacts with CPEB (Nakahata et al 2001).…”

Section: Discussionmentioning

confidence: 99%

Regulated Pumilio-2 binding controls RINGO/Spy mRNA translation and CPEB activation

Padmanabhan¹,

Richter²

2006

Genes Dev.

126

174

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CPEB is a sequence-specific RNA-binding protein that controls the polyadenylation-induced translation of mos and cyclin B1 mRNAs in maturing Xenopus oocytes. CPEB activity requires not only the phosphorylation of S174, but also the synthesis of a heretofore-unknown upstream effector molecule. We show that the synthesis of RINGO/Spy, an atypical activator of cyclin-dependent kinases (cdks), is necessary for CPEB-directed polyadenylation. Deletion analysis and mRNA reporter assays show that a cis element in the RINGO/Spy 3 UTR is necessary for translational repression in immature (G2-arrested) oocytes. The repression is mediated by 3 UTR Pumilio-Binding Elements (PBEs), and by its binding protein Pumilio 2 (Pum2). Pum2 also interacts with the Xenopus homolog of human Deleted for Azoospermia-like (DAZL) and the embryonic poly(A)-binding protein (ePAB). Following the induction of maturation, Pum2 dissociates not only from RINGO/Spy mRNA, but from XDAZL and ePAB as well; as a consequence, RINGO/Spy mRNA is translated. These results demonstrate that a reversible Pum2 interaction controls RINGO/Spy mRNA translation and, as a result, CPEB-mediated cytoplasmic polyadenylation.

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Section: Discussionmentioning

confidence: 99%

Regulated Pumilio-2 binding controls RINGO/Spy mRNA translation and CPEB activation

Padmanabhan¹,

Richter²

2006

Genes Dev.

126

174

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“…The interactions between hNanos1 and several partners could be essential for the functions of this molecule. In Drosophila, nanos is recruited by pumilio to bind to nanos-responsive elements located in the 3 0 untranslated region of target transcripts, for example, hunchback and cyclin B mRNAs (Murata and Wharton, 1995;Asaoka-Taguchi et al, 1999;Sonoda and Wharton, 2001). The structure of pumilio reveals the presence of a Puf domain containing helical repeats (PUM repeats) and showing homology with armadillo-repeat domains (Edwards et al, 2001).…”

Section: Regulation Of Mt1-mmp By Hnanos1mentioning

confidence: 99%

The E-cadherin-repressed hNanos1 gene induces tumor cell invasion by upregulating MT1-MMP expression

et al. 2008

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In this study, we examined the role of the E-cadherinrepressed gene human Nanos1 (hNanos1) in tumor invasion process. First, our in vivo study revealed that hNanos1 mRNAs were overexpressed in invasive lung carcinomas. Moreover, hNanos1 was co-localized with MT1-MMP (membrane type 1-matrix metalloproteinase) in E-cadherin-negative invasive lung tumor clusters. Using an inducible Tet-on system, we showed that induction of hNanos1 expression in DLD1 cells increased their migratory and invasive abilities in a three-dimensional migration and in a modified Boyden chamber assay. Accordingly, we demonstrated that hNanos1 upregulated MT1-MMP expression at the mRNA and protein levels. Inversely, using an RNA interference strategy to inhibit hNanos1 expression in invasive Hs578T, BT549 and BZR cancer cells, we observed a downregulation of MT1-MMP mRNA and protein and concomitantly a decrease of the invasive capacities of tumor cells in a modified Boyden chamber assay. Taken together, our results demonstrate that hNanos1, by regulating MT1-MMP expression, plays an important role in the acquisition of invasive properties by epithelial tumor cells.

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“…APUM5 contains the Pumilio-homology domain (PHD) and encodes a putative Puf, which was originally identified in Drosophila melanogaster and Caenorhabditis elegans (6). Pufs are highly conserved in various organisms and work as posttranscriptional and translational repressors (7,8). PHD has RNA binding activity; there are eight repeats with three alpha helices in each repeat.…”

mentioning

confidence: 99%

ArabidopsisPumilio protein APUM5 suppressesCucumber mosaic virusinfection via direct binding of viral RNAs

Huh¹,

Kim

Paek

2012

Proc. Natl. Acad. Sci. U.S.A.

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Posttranscriptional/translational regulation of gene expression is mediated by diverse RNA binding proteins and plays an important role in development and defense processes. Among the RNAbinding proteins, the mammalian Pumilio RNA-binding family (Puf) acts as posttranscriptional and translational repressors. An Arabidopsis Puf mutant, apum5-D, was isolated during a T-DNA insertional mutant screen for mutants with reduced susceptibility to Cucumber mosaic virus (CMV) infection. Interestingly, CMV RNA contained putative Pumilio-homology domain binding motifs in its 3′ untranslated region (UTR) and internal places in its genome. APUM5 directly bound to the 3′ UTR motifs and some internal binding motifs in CMV RNAs in vitro and in vivo. We showed that APUM5 acts as a translational repressor that regulates the 3′ UTR of CMV and affects CMV replication. This study uncovered a unique defense system that Arabidopsis APUM5 specifically regulates CMV infection by the direct binding of CMV RNAs. plant defense | Pumilio RNA binding protein | TuMV P lant viruses are the obligate pathogens, and host proteins facilitate the multiplication of viruses by affecting processes such as viral replication, cell-to-cell movement, and systemic movement of the virus (1). These processes occur upon the interaction between the virus and host proteins or after the suppression of the host basal defense mechanism and often lead to abnormal phenotypes of virus-infected host plants, such as small, highly branched bushes with deformed leaves, stunting, and reduced apical dominance (2-4). Thus, the reduced growth and developmental changes in the virus-infected plants are typical symptoms of virus infection and signify that the virus has undergone a successful life cycle. To understand the molecular mechanisms underlying viral multiplication and symptoms in plants, it is necessary to identify and characterize the host factors involved in these processes.To identify novel host factors involved in the multiplication of plant RNA viruses in susceptible plants, T-DNA insertion mutants of Arabidopsis thaliana Col-0 ecotype, in which CMVKor multiplication is abrogated (5), were screened. An Arabidopsis Puf mutant, apum5-D, in which Cucumber mosaic virus (CMV) multiplication was affected during viral spreading, was isolated. APUM5 contains the Pumilio-homology domain (PHD) and encodes a putative Puf, which was originally identified in Drosophila melanogaster and Caenorhabditis elegans (6). Pufs are highly conserved in various organisms and work as posttranscriptional and translational repressors (7,8). PHD has RNA binding activity; there are eight repeats with three alpha helices in each repeat. The inner surface of the PHD binds the RNA. The outer surface of the domain permits protein-protein interactions with diverse proteins, such as deadenylase and general translation factors (9, 10). Arabidopsis Pufs also exhibit RNA-binding activity and have conserved binding motifs (11,12). However, plant Puf functions have not yet been fully identified or charact...

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Drosophila Brain Tumor is a translational repressor

Cited by 295 publications

References 52 publications

Regulated Pumilio-2 binding controls RINGO/Spy mRNA translation and CPEB activation

Regulated Pumilio-2 binding controls RINGO/Spy mRNA translation and CPEB activation

The E-cadherin-repressed hNanos1 gene induces tumor cell invasion by upregulating MT1-MMP expression

ArabidopsisPumilio protein APUM5 suppressesCucumber mosaic virusinfection via direct binding of viral RNAs

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