Sm protein methylation is dispensable for snRNP assembly in <i>Drosophila melanogaster</i>

Gonsalvez, Graydon B.; Praveen, Kavita; Hicks, Amanda J.; Tian, Liang; Matera, A. Gregory

doi:10.1261/rna.940708

Cited by 42 publications

(40 citation statements)

References 40 publications

(56 reference statements)

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“…PRMT7 belongs to the type II methyltransferase capable of generating symmetric dimethyl-arginine (SDMA) modifications of proteins (19). It has been indicated that PRMT7 may participate in a variety of physiologic processes, e.g., PRMT7 plays a role in male imprinted gene methylation by catalyzing H4R3me2s (20), and the SnRNP assembly and biogenesis are thought to be mediated by PRMT7 via posttranslational modification (21). Also, PRMT7 is involved in regulation of the DNA damage repair genes by mediating H2AR3me2s and H4R3me2s (22).…”

Section: Introductionmentioning

confidence: 99%

PRMT7 Induces Epithelial-to-Mesenchymal Transition and Promotes Metastasis in Breast Cancer

et al. 2014

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Epithelial-to-mesenchymal transition (EMT) enables metastasis. E-cadherin loss is a hallmark of EMT, but there remains an incomplete understanding of the epigenetics of this process. The protein arginine methyltransferase PRMT7 functions in various physiologic processes, including mRNA splicing, DNA repair, and neural differentiation, but its possible roles in cancer and metastasis have not been explored. In this report, we show that PRMT7 is expressed at higher levels in breast carcinoma cells and that elevated PRMT7 mediates EMT and metastasis. PRMT7 could inhibit the expression of E-cadherin by binding to its proximal promoter in a manner associated with altered histone methylation, specifically with elevated H4R3me2s and reduced H3K4me3, H3Ac, and H4Ac, which occurred at the E-cadherin promoter upon EMT induction. Moreover, PRMT7 interacted with YY1 and HDAC3 and was essential to link these proteins to the E-cadherin promoter. Silencing PRMT7 restored E-cadherin expression by repressing H4R3me2s and by increasing H3K4me3 and H4Ac, attenuating cell migration and invasion in MDA-MB-231 breast cancer cells. Overall, our results define PRMT7 as an inducer of breast cancer metastasis and present the opportunity for applying PRMT7-targeted therapeutics to treat highly invasive breast cancers. Cancer Res; 74(19); 5656-67. Ó2014 AACR.

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Section: Introductionmentioning

confidence: 99%

PRMT7 Induces Epithelial-to-Mesenchymal Transition and Promotes Metastasis in Breast Cancer

et al. 2014

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“…Although protozoa, yeast and even models such as Drosophila, can be advantageous in studying biological processes such as snRNP assembly [44,59,60], results obtained with such model organisms should be interpreted with caution in regards to SMA pathogenesis. In these models, snRNP assembly may function by different mechanisms owing to ortholog divergence of proteins, which can be quite significant in certain models [44].…”

Section: Small Nuclear Ribonucleoprotein Assemblymentioning

confidence: 99%

The many faces of SMN: deciphering the function critical to spinal muscular atrophy pathogenesis

2010

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Spinal muscular atrophy (SMA) is the leading genetic cause of infant death, affecting 1 in 6000-10,000 live births. SMA is an autosomal recessive disorder characterized by the degeneration of a-motor neurons, and lower limb and proximal muscle weakness and wasting. SMA is the result of the deletion of or mutations in the survival motor neuron (SMN)1 gene. Currently, our understanding of how loss of the widely expressed SMN leads to the selective pathogenesis observed in SMA is limited. Here, we discuss the known nuclear and cytoplasmic functions of the SMN protein and how they relate to the SMA pathology reported in motor neurons, striated muscle and at neuromuscular junctions. While a vast amount of work in various cell and animal models has increased our knowledge of the many functions of the SMN protein, we have yet to come to a full understanding of which role(s) are central to SMA pathogenesis.Keywords n actin dynamics n neurodegeneration n preclinical models n snRNP assembly n spinal muscular atrophy n survival motor neuron ReviewFor reprint orders, please contact: reprints@futuremedicine.com

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“…The requirement for methylation in snRNP assembly has been recently tested in Drosophila. The use of two distinct lines that synthesise modified isoforms of SmD1, in which either the entire RG-rich tail is deleted or the arginine residues are substituted by lysine, shows that in Drosophila the RG-rich tail of SmD1 is required for cell viability, whereas the symmetric dimethylation of C-terminal arginine residues in SmD1 is required neither for viability nor for snRNP assembly (Gonsalvez et al, 2008). These data suggest that the sDMA modification of SmD1 is dispensable for snRNP particle assembly.…”

Section: Introductionmentioning

confidence: 99%

“…In csul animals, the major Sm-class snRNPs are expressed normally (Gonsalvez et al, 2006), suggesting that csul is dispensable for snRNP assembly in Drosophila. In addition, flies express an orthologue of PRMT7, Dart7 (Art7, CG9882) (Boulanger et al, 2004), which is also required for sDMA modification of Sm proteins in vivo (Gonsalvez et al, 2008). Unlike csul, Dart7 is an essential gene (Gonsalvez et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

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Arginine methylation of SmB is required for Drosophila germ cell development

Anne

2010

Development

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SUMMARYSm proteins constitute the common core of spliceosomal small nuclear ribonucleoproteins. Although Sm proteins are known to be methylated at specific arginine residues within the C-terminal arginine-glycine dipeptide (RG) repeats, the biological relevance of these modifications remains unknown. In this study, a tissue-specific function of arginine methylation of the SmB protein was identified in Drosophila. Analysis of the distribution of SmB during oogenesis revealed that this protein accumulates at the posterior pole of the oocyte, a cytoplasmic region containing the polar granules, which are necessary for the formation of primordial germ cells. The pole plasm localisation of SmB requires the methylation of arginine residues in its RG repeats by the Capsuléen-Valois methylosome complex. Functional studies showed that the methylation of these arginine residues is essential for distinct processes of the germline life cycle, including germ cell formation, migration and differentiation. In particular, the methylation of a subset of these arginine residues appears essential for the anchoring of the polar granules at the posterior cortex of the oocyte, whereas the methylation of another subset controls germ cell migration during embryogenesis. These results demonstrate a crucial role of arginine methylation in directing the subcellular localisation of SmB and that this modification contributes specifically to the establishment and development of germ cells.

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Sm protein methylation is dispensable for snRNP assembly in Drosophila melanogaster

Cited by 42 publications

References 40 publications

PRMT7 Induces Epithelial-to-Mesenchymal Transition and Promotes Metastasis in Breast Cancer

PRMT7 Induces Epithelial-to-Mesenchymal Transition and Promotes Metastasis in Breast Cancer

The many faces of SMN: deciphering the function critical to spinal muscular atrophy pathogenesis

Arginine methylation of SmB is required for Drosophila germ cell development

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