On track with P-bodies

Kulkarni, Meeta G.; Ozgur, Sevim; Stoecklin, Georg

doi:10.1042/bst0380242

Cited by 177 publications

(167 citation statements)

References 95 publications

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“…processing bodies (P-bodies, PBs or GW/P-bodies) that in mammalian cultured cells are known to be involved in the posttranscriptional control of mRNAs through mRNA degradation, transport, stabilisation and translational repression (Kulkarni et al 2010).…”

Section: Pachytene Pirnasmentioning

confidence: 99%

Chromatoid body and small RNAs in male germ cells

Meikar¹,

Ros²,

Korhonen³

et al. 2011

Reproduction

143

154

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The chromatoid body (CB) is a germ granule in the cytoplasm of postmeiotic haploid round spermatids that is loaded with RNA and RNAbinding proteins. Following the discovery of small non-coding RNA-mediated gene regulation and the identification of PIWI-interacting RNAs (piRNAs) that have crucial roles in germ line development, the function of the CB has slowly begun to be revealed. Male germ cells utilise small RNAs to control the complex and specialised process of sperm production. Several microRNAs have been identified during spermatogenesis. In addition, a high number of piRNAs are present both in embryonic and postnatal male germ cells, with their expression being impressively induced in late meiotic cells and haploid round spermatids. At postmeiotic stage of germ cell differentiation, the CB accumulates piRNAs and proteins of piRNA machinery, as well as several other proteins involved in distinct RNA regulation pathways. All existing evidence suggests a role for the CB in mRNA regulation and small RNA-mediated gene control, but the mechanisms remain uncharacterised. In this review, we summarise the current knowledge of the CB and its association with small RNA pathways.

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Section: Pachytene Pirnasmentioning

confidence: 99%

Chromatoid body and small RNAs in male germ cells

Meikar¹,

Ros²,

Korhonen³

et al. 2011

Reproduction

143

154

View full text Add to dashboard Cite

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“…Transcripts that are not translated or targeted for degradation are directed to "P-bodies" (processing bodies) and stress granules to compartmentalise the mRNA pool, which is also a mechanism for post-transcriptional control of gene expression (Kulkarni et al 2010). TcD-HH1 is a DEAD-box RNA helicase that can also localise to cytoplasmic stress granules (Holetz et al 2007) and proteins that are involved in translation, metabolism, cytoskeleton assembly or heat-shock defence can associate directly or indirectly with TcDHH1.…”

Section: Rna-binding Proteins Are Essential Trans-acting Elements Formentioning

confidence: 99%

Regulatory elements involved in the post-transcriptional control of stage-specific gene expression in Trypanosoma cruzi: a review

Araújo

Teixeira

2011

Mem. Inst. Oswaldo Cruz

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Trypanosoma cruzi is an intracellular parasite that is transmitted by at least 40 different blood-sucking triatomine species to over 1,000 mammalian species (Brener et al. 2000). This parasite must adapt to enormous changes in its extracellular milieu, such as changes in environmental temperature as well as in the available nutrients inside each host. The parasite has a complex life cycle that is characterised by four stages; epimastigotes and metacyclic trypomastigotes are present in the insect vector, whereas intracellular amastigotes and bloodstream trypomastigotes are present in the mammalian host. Thus, this species must develop a broad set of molecular tools that allow it to multiply in the insect gut, to invade and multiply inside a large number of distinct mammalian cell types and to circumvent host immune defence systems. To meet such phenotypic plasticity, T. cruzi relies on unique mechanisms that can control the expression of its repertoire of about 12,000 genes. Because its genome is constitutively transcribed into long polycistronic primary transcripts, mRNAs for proteincoding genes must be processed through trans-splicing and polyadenylation reactions. The mRNAs must also interact with different protein factors in a complex posttranscriptional regulatory machinery that determines the levels of their protein product according to the cellular demands of the parasite in each stage of its life cycle.In the same issue that the T. cruzi genome was published (El-Sayed et al. 2005a), a study describing its proteome was also reported (Atwood et al. 2005). Proteins extracted from whole-cell and subcellular lysates of the four stages of T. cruzi were analysed by mass spectrometry (epimastigotes, metacyclic trypomastigotes, amastigotes and trypomastigotes), which identified 2,784 proteins belonging to the 1,168 protein groups in the annotated T. cruzi genome. Although about 30% of the identified proteins were found at all life-cycle stages, at least 248 proteins were only expressed at one stage, thereby demonstrating significant changes in the relative abundance of T. cruzi proteins throughout its life cycle. One of the main findings in these proteomic analyses was that the four parasite stages use distinct energy sources (Atwood et al. 2005); intracellular amastigotes upregulated proteins involved in lipid-dependent energy metabolism, such as enzymes of the citric acid cycle, whereas enzymes capable of catalysing the conversion of histidine to glutamate were more abundant in the insect epimastigote stage. Heat-shock proteins (HSP) and proteins involved in vesicular trafficking were also preferentially detected in amastigotes. Furthermore, enzymes involved in antioxidant defence were upregulated during the transformation of epimastigotes into invasive metacyclic trypomastigotes, whereas bloodstream trypomastigotes upregulated the surface expression of several large gene families that are known to be involved in interacting with the mammalian host (Atwood et al. 2005).In agreement with this proteomics data, glo...

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“…Stationary PBs associate with actin bundles whereas mobile PBs connect to the microtubule network, 36,39,40 and these contact sites may be disrupted by active RhoA signaling and activation of specific downstream effector proteins. Alternatively, the formation of particular F-actin structures such as stress fibers may place a mechanical strain on the linkage between PB and cytoskeletal structures, mediating their dissociation.…”

Section: Modelmentioning

confidence: 99%

“…37,38 PBs also maintain a dynamic relationship with the cytoskeleton; stationary PBs associate with actin bundles whereas mobile PBs connect to the microtubule network. 36,39,40 Though PB formation was recently shown to be modified by the cytoskeletal regulator RhoA, 22,27,28 the precise mechanism of action remains to be elucidated.…”

Section: Processing Bodies Control Inflammatory Mediator Release By Ecsmentioning

confidence: 99%