Smaug, a novel and conserved protein, contributes to repression of nanos mRNA translation in vitro

Smibert, Craig; Lie, Yung S.; Shillinglaw, Wendy; Henzel, William J.; Macdonald, Paul M.

doi:10.1017/s1355838299991392

Cited by 133 publications

(148 citation statements)

References 60 publications

Supporting

Mentioning

143

Contrasting

Unclassified

Order By: Relevance

“…Notably, TTP knockdown did not influence IL-8 levels in our screen, presumably because it is not expressed in HEK cells (60). Similarly, silencing the RNA-binding protein SAMD4 enhanced IL-8 secretion, consistent with its published role in binding and destabilizing mRNA (61) and the presence of six consensus SAMD4 recognition elements in the 3Ј-UTR of IL-8 (62). Increasing our understanding of the various cellular mechanisms that influence IL-8 production and secretion is an important step forward in developing strategies to manipulate IL-8 levels for potential therapeutic applications.…”

Section: Discussionsupporting

confidence: 70%

A Genome-wide Small Interfering RNA (siRNA) Screen Reveals Nuclear Factor-κB (NF-κB)-independent Regulators of NOD2-induced Interleukin-8 (IL-8) Secretion

Warner

Burberry

Pliakas

et al. 2014

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: Interleukin-8 (IL-8) is a potent proinflammatory cytokine. Results: We identify many regulators of IL-8 secretion induced by the pattern recognition receptor NOD2. Conclusion: Many diverse cellular processes, including protein ubiquitination and trafficking, specifically affect IL-8 secretion. Significance: The identified regulators, particularly those present in inflammatory disease loci, reveal molecular targets for therapeutic modulation of IL-8.

show abstract

Section: Discussionsupporting

confidence: 70%

A Genome-wide Small Interfering RNA (siRNA) Screen Reveals Nuclear Factor-κB (NF-κB)-independent Regulators of NOD2-induced Interleukin-8 (IL-8) Secretion

Warner

Burberry

Pliakas

et al. 2014

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…The protein is a homolog of the Drosophila protein Smaug, a translational repressor that mediates body pattering during embryogenesis by binding to a mRNA hairpin termed Smaug recognition element (SRE) [41]. The SRE hairpin exhibits consensus sequences 5′-UNGA-N and 5′-GNGC-N which are targeted by α-helical sterile alpha motif (SAM) domain of Vts1p, a domain also implicated in protein-protein and DNAprotein interactions [42].…”

Section: Specific Recognition Of Rna Loops By Proteinsmentioning

confidence: 99%

Towards deciphering the principles underlying an mRNA recognition code

Serganov

Patel

2008

Current Opinion in Structural Biology

View full text Add to dashboard Cite

Messenger RNAs interact with a number of different molecules that determine the fate of each transcript and contribute to the overall pattern of gene expression. These interactions are governed by specific mRNA signals, which in principle could represent a special mRNA recognition 'code'. Both, small molecules and proteins demonstrate a diversity of mRNA binding modes often dependent on the structural context of the regions surrounding specific target sequences. In this review, we have highlighted recent structural studies that illustrate the diversity of recognition principles used by mRNA binders for timely and specific targeting and processing of the message.

show abstract

“…The Smaug (Smg) family is a class of proteins, conserved from yeast to humans, that regulate gene expression posttranscriptionally through their ability to bind directly to target mRNAs (Smibert et al 1996(Smibert et al , 1999Dahanukar et al 1999;Aviv et al 2003;Baez and Boccaccio 2005;Semotok et al 2005). Family members bind RNA with similar specificity through a conserved sterile alpha motif (SAM) domain that is able to interact with stem-loop structures termed Smg recognition elements (SREs) (Smibert et al 1996(Smibert et al , 1999Dahanukar et al 1999;Crucs et al 2000;Aviv et al 2003;Green et al 2003).…”

Section: Introductionmentioning

confidence: 99%

S. cerevisiae Vts1p induces deadenylation-dependent transcript degradation and interacts with the Ccr4p-Pop2p-Not deadenylase complex

Rendl¹,

Bieman²,

Smibert³

2008

RNA

Self Cite

View full text Add to dashboard Cite

The Smaug family of sequence-specific RNA binding proteins regulates mRNA translation and degradation by binding to consensus stem-loop structures in target mRNAs. Vts1p is a member of the Smaug protein family that regulates the stability of target transcripts in Saccharomyces cerevisiae. Here we focus on the mechanism of Vts1p-mediated mRNA decay. Using RNA reporters that recapitulate Vts1p-mediated decay in vivo, we demonstrate that Vts1p stimulates mRNA degradation through deadenylation mediated by the Ccr4p-Pop2p-Not deadenylase complex. We also show that Vts1p interacts with the Ccr4p-Pop2p-Not complex suggesting that Vts1p recruits the Ccr4p-Pop2p-Not deadenylase complex to target mRNAs, resulting in transcript decay. Following deadenylation Vts1p target transcripts are decapped and subsequently degraded by the 59-to-39 exonuclease Xrn1p. Decapping and 59-to-39 decay is thought to occur in foci known as P-bodies, and we provide evidence that Vts1p function may involve P-bodies. Taken together with previous work, these data suggest that Smaug family members employ a conserved mechanism to induce transcript degradation that involves recruitment of the Ccr4-Pop2-Not deadenylase to target mRNAs.

show abstract

Smaug, a novel and conserved protein, contributes to repression of nanos mRNA translation in vitro

Cited by 133 publications

References 60 publications

A Genome-wide Small Interfering RNA (siRNA) Screen Reveals Nuclear Factor-κB (NF-κB)-independent Regulators of NOD2-induced Interleukin-8 (IL-8) Secretion

A Genome-wide Small Interfering RNA (siRNA) Screen Reveals Nuclear Factor-κB (NF-κB)-independent Regulators of NOD2-induced Interleukin-8 (IL-8) Secretion

Towards deciphering the principles underlying an mRNA recognition code

S. cerevisiae Vts1p induces deadenylation-dependent transcript degradation and interacts with the Ccr4p-Pop2p-Not deadenylase complex

Contact Info

Product

Resources

About