PMID:20659974

Citation	Anne, J (2010) Arginine methylation of SmB is required for Drosophila germ cell development. Development 137:2819-28
Abstract	Sm 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.
Links	PubMed Online version:10.1242/dev.052944
Keywords	Animals; Animals, Genetically Modified; Arginine/metabolism; Cell Polarity; Drosophila/embryology; Drosophila/genetics; Drosophila/metabolism; Drosophila Proteins/chemistry; Drosophila Proteins/genetics; Drosophila Proteins/metabolism; Green Fluorescent Proteins/genetics; Green Fluorescent Proteins/metabolism; Methylation; Models, Biological; Mutagenesis, Site-Directed; Oocytes/metabolism; Oogenesis/genetics; Oogenesis/physiology; Recombinant Fusion Proteins/chemistry; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/metabolism; Ribonucleoproteins, Small Nuclear/chemistry; Ribonucleoproteins, Small Nuclear/genetics; Ribonucleoproteins, Small Nuclear/metabolism; Subcellular Fractions/metabolism
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
DROME:SMD3	located_in	GO:0045495: pole plasm	ECO:0000314: direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
DROME:TUD	located_in	GO:0045495: pole plasm	ECO:0000314: direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
DROME:TUD	located_in	GO:0005737: cytoplasm	ECO:0000314: direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
DROME:TUD	located_in	GO:0043186: P granule	ECO:0000314: direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
DROME:RSMB	located_in	GO:0015030: Cajal body	ECO:0000314: direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
DROME:RSMB	located_in	GO:0045495: pole plasm	ECO:0000314: direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
DROME:RSMB	located_in	GO:0005634: nucleus	ECO:0000314: direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
DROME:RSMB	involved_in	GO:0008406: gonad development	ECO:0000315: mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
DROME:RSMB	involved_in	GO:0007281: germ cell development	ECO:0000315: mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete

References

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