Drosophila Decapping Protein 1, dDcp1, Is a Component of the oskar mRNP Complex and Directs Its Posterior Localization in the Oocyte

Lin, Ming-Der; Fan, Shih‐Jung; Hsu, W. Siang; Chou, Tze-Bin

doi:10.1016/j.devcel.2006.02.021

Cited by 87 publications

(120 citation statements)

References 62 publications

(89 reference statements)

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“…3B). Staining of Dnmt2 genTG-EGFP ovaries with an antibody to ME31B, a Drosophila RNA processing body component in the germline (Lin et al 2006), also showed processing body signals after heat shock with strong colocalization of Dnmt2 and ME31B (Fig. 3C).…”

Section: Resultsmentioning

confidence: 88%

RNA methylation by Dnmt2 protects transfer RNAs against stress-induced cleavage

Schaefer¹,

Pollex²,

Hanna³

et al. 2010

Genes Dev.

620

682

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Dnmt2 proteins are the most conserved members of the DNA methyltransferase enzyme family, but their substrate specificity and biological functions have been a subject of controversy. We show here that, in addition to tRNA Asp-GTC , tRNA Val-AAC and tRNA Gly-GCC are also methylated by Dnmt2. Drosophila Dnmt2 mutants showed reduced viability under stress conditions, and Dnmt2 relocalized to stress granules following heat shock. Strikingly, stress-induced cleavage of tRNAs was Dnmt2-dependent, and Dnmt2-mediated methylation protected tRNAs against ribonuclease cleavage. These results uncover a novel biological function of Dnmt2-mediated tRNA methylation, and suggest a role for Dnmt2 enzymes during the biogenesis of tRNA-derived small RNAs.Supplemental material is available at http://www.genesdev.org.

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Section: Resultsmentioning

confidence: 88%

RNA methylation by Dnmt2 protects transfer RNAs against stress-induced cleavage

Schaefer¹,

Pollex²,

Hanna³

et al. 2010

Genes Dev.

620

682

View full text Add to dashboard Cite

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“…Second, the Argonaute I homolog from sea urchins, Seawi, has been identified as a microtubule-associated protein and localizes in cytoplasmic puncta (Rodriguez et al 2005). Third, the oskar mRNP in Drosophilia oocytes, which contains several P-body proteins, mislocalizes in mutants in which microtubule organization is abnormal (Lin et al 2006). While a precise function for P-bodies in mRNA metabolism remains ambiguous, taken together, these results suggest that P-bodies and similar mRNP granular structures are influenced by the microtubule network in the cell, and P-body assembly is not obligatorily dependent on global alterations in mRNA metabolism.…”

Section: Discussionmentioning

confidence: 99%

Microtubule disruption stimulates P-body formation

Sweet¹,

Boyer²,

Hu³

et al. 2007

RNA

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Processing bodies (P-bodies) are subcellular ribonucleoprotein (RNP) granules that have been hypothesized to be sites of mRNA degradation, mRNA translational control, and/or mRNA storage. Importantly, P-bodies are conserved from yeast to mammals and contain a common set of evolutionarily conserved protein constituents. P-bodies are dynamic structures and their formation appears to fluctuate in correlation with alterations in mRNA metabolism. Despite these observations, little is understood about how P-body structures are formed within the cell. In this study, we demonstrate a relationship between P-bodies and microtubules in the budding yeast, Saccharomyces cerevisiae. First, we demonstrate that disruption of microtubules by treatment with the drug benomyl leads to aggregation of P-body components. Consistent with this finding, we also demonstrate that disruption of microtubules by a temperature-sensitive allele of the major a tubulin, TUB1 (tub1-724) stimulates P-body formation. Second, we find that the a-tubulin protein Tub1 colocalizes with P-bodies upon microtubule destabilization. Third, we determine that a putative tubulin tyrosine ligase, encoded by YBR094W, is a protein component of P-bodies, providing additional evidence for a physical connection between P-bodies and microtubules. Finally, we establish that P-bodies formed by microtubule destabilization fail to correlate with global changes in the stability of mRNA or in general mRNA translation. These findings demonstrate that the aggregation of P-body components is linked to the intracellular microtubule network, and, further, that P-bodies formed by disruption of microtubules aggregate independent of broad alterations in either mRNA decay or mRNA translation.

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“…Thus, mRNA decay blocks could also affect germ granules and neuronal transport granules, with which P-bodies also physically interact. 14,15 Notably, various mRNA degradative enzymes are found in mRNP granules besides P-bodies, such as Xrn1 in stress granules 11 and Drosophila/mouse spermatid nuage, 65 Dcp1/ Dcp2 in various germ granules, [66][67][68] and several Argonaute proteins with endonuclease activity in stress granules, 69 and various germ granules. [70][71][72][73] Whether mRNA degradation occurs in mRNP granules besides P-bodies remains poorly studied.…”

Section: Mrnp Granules Assemble Via Common Mechanismsmentioning

confidence: 99%