title: Nessun Dorma, a novel centralspindlin partner, is required for cytokinesis in Drosophila spermatocytes.
abstract: Cytokinesis, the final step of cell division, usually ends with the abscission of the two daughter cells. In some tissues, however, daughter cells never completely separate and remain interconnected by intercellular bridges or ring canals. In this paper, we report the identification and analysis of a novel ring canal component, Nessun Dorma (Nesd), isolated as an evolutionarily conserved partner of the centralspindlin complex, a key regulator of cytokinesis. Nesd contains a pectin lyase-like domain found in proteins that bind to polysaccharides, and we present evidence that it has high affinity for β-galactosides in vitro. Moreover, nesd is an essential gene in Drosophila melanogaster, in which it is required for completion of cytokinesis during male meiosis and possibly in female germline cells. Our findings indicate that Nesd is a novel carbohydrate-binding protein that functions together with centralspindlin in late cytokinesis, thus highlighting the importance of glycosylation in this process.
authors.affiliation: Department of Pathology, University of Cambridge, Cambridge CB2 1QP, England, UK.
authors.forename: Emilie
authors.initials: E
authors.lastname: Montembault
authors.forename: Wei
authors.initials: W
authors.lastname: Zhang
authors.forename: Marcin R
authors.initials: MR
authors.lastname: Przewloka
authors.forename: Vincent
authors.initials: V
authors.lastname: Archambault
authors.forename: Emeric W
authors.initials: EW
authors.lastname: Sevin
authors.forename: Ernest D
authors.initials: ED
authors.lastname: Laue
authors.forename: David M
authors.initials: DM
authors.lastname: Glover
authors.forename: Pier Paolo
authors.initials: PP
authors.lastname: D'Avino
mesh_terms: D000199:Actins / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D003285:Contractile Proteins / Q000378:metabolism; D048749:Cytokinesis / Q000502:physiology*; D029721:Drosophila Proteins / Q000235:genetics / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000166:cytology* / Q000502:physiology*; D005260:Female; D020690:GTPase-Activating Proteins / Q000235:genetics / Q000378:metabolism; D005697:Galactosides / Q000378:metabolism; D005854:Germ Cells / Q000166:cytology / Q000378:metabolism; D006801:Humans; D008297:Male; D008540:Meiosis / Q000502:physiology*; D008869:Microtubule-Associated Proteins / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D046912:Multiprotein Complexes / Q000378:metabolism; D024462:Myosin Type II / Q000235:genetics / Q000378:metabolism; D010446:Peptide Fragments / Q000235:genetics / Q000378:metabolism; D010802:Phylogeny; D011134:Polysaccharides / Q000378:metabolism; D011485:Protein Binding / Q000502:physiology; D054730:Protein Interaction Domains and Motifs / Q000502:physiology; D013090:Spermatocytes / Q000166:cytology* / Q000378:metabolism; D008941:Spindle Apparatus / Q000378:metabolism*; D013692:Telophase / Q000502:physiology
chemical_list: D000199:Actins; D003285:Contractile Proteins; D029721:Drosophila Proteins; D020690:GTPase-Activating Proteins; D005697:Galactosides; C092935:KIF23 protein, human; D008869:Microtubule-Associated Proteins; D046912:Multiprotein Complexes; C556093:Nesd protein, Drosophila; D010446:Peptide Fragments; D011134:Polysaccharides; C495593:Sqh protein, Drosophila; C095886:anillin; C007816:beta-galactoside; C490516:pav protein, Drosophila; C502951:tum protein, Drosophila; D024462:Myosin Type II