Valois, a component of the nuage and pole plasm, is involved in assembly of these structures, and binds to Tudor and the methyltransferase Capsuléen

Anne, Joël; Mechler, Bernard M.

doi:10.1242/dev.01809

Cited by 59 publications

(76 citation statements)

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“…Probing similar protein blots with the anti-ASYM24 antibodies, which identify proteins containing asymmetric di-methyl arginyl residues (aDMA) (Boisvert et al, 2002), we found no change in the pattern of the reactive protein bands in all extracts. These results corroborate our finding that Csul and Vls are part of a methylosome complex contributing to sDMA synthesis in specific proteins (Anne and Mechler, 2005), and indicate that Vls acts as a co-factor of Csul. Moreover, these data show that Vas, Osk and Aub exert no function in the Csul-dependent synthesis of sDMA residues.…”

Section: Sm Proteins Are Substrates Of the Csul-vls Complexsupporting

confidence: 91%

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Arginine methyltransferase Capsuléen is essential for methylation of spliceosomal Sm proteins and germ cell formation inDrosophila

et al. 2007

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Although arginine modification has been implicated in a number of cellular processes, the in vivo requirement of protein arginine methyltransferases (PRMTs) in specific biological processes remain to be clarified. In this study we characterize the Drosophila PRMT Capsuléen, homologous to human PRMT5. During Drosophila oogenesis, catalytic activity of Capsuléen is necessary for both the assembly of the nuage surrounding nurse cell nuclei and the formation of the pole plasm at the posterior end of the oocyte. In particular, we show that the nuage and pole plasm localization of Tudor, an essential component for germ cell formation, are abolished in csul mutant germ cells. We identify the spliceosomal Sm proteins as in vivo substrates of Capsuléen and demonstrate that Capsuléen, together with its associated protein Valois, is essential for the synthesis of symmetric di-methylated arginyl residues in Sm proteins. Finally, we show that Tudor can be targeted to the nuage in the absence of Sm methylation by Capsuléen, indicating that Tudor localization and Sm methylation are separate processes. Our results thus reveal the role of a PRMT in protein localization in germ cells.

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Section: Sm Proteins Are Substrates Of the Csul-vls Complexsupporting

confidence: 91%

“…To cotranslationally inhibit sDMA synthesis, 0.3 mM S-adenosylhomocysteine (Sigma) was included in the reaction. GST pull-down assays were performed as previously described (Anne and Mechler, 2005).…”

Section: Gst Pull-down Assaymentioning

confidence: 99%

Arginine methyltransferase Capsuléen is essential for methylation of spliceosomal Sm proteins and germ cell formation inDrosophila

et al. 2007

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“…Among these genes are aub, which encodes the piRNAbinding protein Aub (Harris and Macdonald 2001;Brennecke et al 2007;Gunawardane et al 2007); csul/dart5, the Drosophila homolog of PRMT5 (dPRMT5) (Gonsalvez et al 2006;Anne et al 2007); valois, the Drosophila homolog of MEP50 (dMEP50) (Anne and Mechler 2005;Cavey et al 2005); and tudor (Boswell and Mahowald 1985;Lasko 2004, 2005;Arkov et al 2006). In valois-null mutants, dPRMT5 is destabilized, resulting in a loss of sDMA modifications of target proteins, indicating that dMEP50 is required for sDMA production in concert with dPRMT5 (Gonsalvez et al 2006).…”

Section: Introductionmentioning

confidence: 99%

Arginine methylation of Aubergine mediates Tudor binding and germ plasm localization

Kirino¹,

Vourekas²,

Sayed³

et al. 2009

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Piwi proteins such as Drosophila Aubergine (Aub) and mouse Miwi are essential for germline development and for primordial germ cell (PGC) specification. They bind piRNAs and contain symmetrically dimethylated arginines (sDMAs), catalyzed by dPRMT5. PGC specification in Drosophila requires maternal inheritance of cytoplasmic factors, including Aub, dPRMT5, and Tudor (Tud), that are concentrated in the germ plasm at the posterior end of the oocyte. Here we show that Miwi binds to Tdrd6 and Aub binds to Tudor, in an sDMA-dependent manner, demonstrating that binding of sDMA-modified Piwi proteins with Tudor-domain proteins is an evolutionarily conserved interaction in germ cells. We report that in Drosophila tud 1 mutants, the piRNA pathway is intact and most transposons are not de-repressed. However, the localization of Aub in the germ plasm is severely reduced. These findings indicate that germ plasm assembly requires sDMA modification of Aub by dPRMT5, which, in turn, is required for binding to Tudor. Our study also suggests that the function of the piRNA pathway in PGC specification may be independent of its role in transposon control.

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“…Both genes encode crucial components of the methylosome and are required for the assembly of the pole plasm (Anne and Mechler, 2005;Gonsalvez et al, 2006;Anne et al, 2007).…”

Section: Csul/vls-dependent Localisation Of Sm Proteins In the Pole Pmentioning

confidence: 99%

“…Loss of capsuléen (csul; the fly PRMT5 orthologue) activity results in hypomethylation of Sm proteins (Anne and Mechler, 2005;Gonsalvez et al, 2006;Anne et al, 2007). Despite a reduction in sDMA modification of Sm proteins, homozygous csul mutants are viable (Gonsalvez et al, 2006;Anne et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

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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Valois, a component of the nuage and pole plasm, is involved in assembly of these structures, and binds to Tudor and the methyltransferase Capsuléen

Abstract: SummaryValois, a component of the nuage and pole plasm, is involved in assembly of these structures, and binds to Tudor and the methyltransferase Capsuléen

Cited by 59 publications

References 59 publications

Arginine methyltransferase Capsuléen is essential for methylation of spliceosomal Sm proteins and germ cell formation inDrosophila

Arginine methyltransferase Capsuléen is essential for methylation of spliceosomal Sm proteins and germ cell formation inDrosophila

Arginine methylation of Aubergine mediates Tudor binding and germ plasm localization

Arginine methylation of SmB is required for Drosophila germ cell development

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