title: The expression, lamin-dependent localization and RNAi depletion phenotype for emerin in C. elegans.
abstract: Emerin belongs to the LEM-domain family of nuclear membrane proteins, which are conserved in metazoans from C. elegans to humans. Loss of emerin in humans causes the X-linked form of Emery-Dreifuss muscular dystrophy (EDMD), but the disease mechanism is not understood. We have begun to address the function of emerin in C. elegans, a genetically tractable nematode. The emerin gene (emr-1) is conserved in C. elegans. We detect Ce-emerin protein in the nuclear envelopes of all cell types except sperm, and find that Ce-emerin co-immunoprecipitates with Ce-lamin from embryo lysates. We show for the first time in any organism that nuclear lamins are essential for the nuclear envelope localization of emerin during early development. We further show that four other types of nuclear envelope proteins, including fellow LEM-domain protein Ce-MAN1, as well as Ce-lamin, UNC-84 and nucleoporins do not depend on Ce-emerin for their localization. This result suggests that emerin is not essential to organize or localize the only lamin (B-type) expressed in C. elegans. We also analyzed the RNAi phenotype resulting from the loss of emerin function in C. elegans under laboratory growth conditions, and found no detectable phenotype throughout development. We propose that C. elegans is an appropriate system in which to study the molecular mechanisms of emerin function in vivo.
authors.affiliation: Department of Genetics, The Institute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem 91904, Israel.
authors.forename: Yosef
authors.initials: Y
authors.lastname: Gruenbaum
authors.forename: Kenneth K
authors.initials: KK
authors.lastname: Lee
authors.forename: Jun
authors.initials: J
authors.lastname: Liu
authors.forename: Merav
authors.initials: M
authors.lastname: Cohen
authors.forename: Katherine L
authors.initials: KL
authors.lastname: Wilson
mesh_terms: D000818:Animals; D017173:Caenorhabditis elegans / Q000166:cytology / Q000196:embryology* / Q000378:metabolism*; D029742:Caenorhabditis elegans Proteins; D004625:Embryo, Nonmammalian / Q000166:cytology / Q000196:embryology / Q000378:metabolism; D005786:Gene Expression Regulation / Q000502:physiology*; D007797:Laminin / Q000172:deficiency* / Q000235:genetics; D008562:Membrane Glycoproteins / Q000235:genetics / Q000378:metabolism; D008565:Membrane Proteins / Q000172:deficiency* / Q000235:genetics / Q000378:metabolism; D023421:Models, Animal; D020389:Muscular Dystrophy, Emery-Dreifuss / Q000235:genetics / Q000378:metabolism; D009154:Mutation / Q000235:genetics*; D009685:Nuclear Envelope / Q000378:metabolism* / Q000648:ultrastructure; D028861:Nuclear Pore Complex Proteins / Q000235:genetics / Q000378:metabolism; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism; D010641:Phenotype; D012313:RNA / Q000235:genetics / Q000378:metabolism*; D013946:Thymopoietins / Q000172:deficiency* / Q000235:genetics
chemical_list: D029742:Caenorhabditis elegans Proteins; D007797:Laminin; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D028861:Nuclear Pore Complex Proteins; D009687:Nuclear Proteins; D013946:Thymopoietins; C120560:Unc-84 protein, C elegans; C092710:emerin; C485768:lem-2 protein, C elegans; D012313:RNA