title: BAF is required for emerin assembly into the reforming nuclear envelope.
abstract: Mutations in emerin cause the X-linked recessive form of Emery-Dreifuss muscular dystrophy (EDMD). Emerin localizes at the inner membrane of the nuclear envelope (NE) during interphase, and diffuses into the ER when the NE disassembles during mitosis. We analyzed the recruitment of wildtype and mutant GFP-tagged emerin proteins during nuclear envelope assembly in living HeLa cells. During telophase, emerin accumulates briefly at the 'core' region of telophase chromosomes, and later distributes over the entire nuclear rim. Barrier-to-autointegration factor (BAF), a protein that binds nonspecifically to double-stranded DNA in vitro, co-localized with emerin at the 'core' region of chromosomes during telophase. An emerin mutant defective for binding to BAF in vitro failed to localize at the 'core' in vivo, and subsequently failed to localize at the reformed NE. In HeLa cells that expressed BAF mutant G25E, which did not show 'core' localization, the endogenous emerin proteins failed to localize at the 'core' region during telophase, and did not assemble into the NE during the subsequent interphase. BAF mutant G25E also dominantly dislocalized LAP2beta and lamin A from the NE, but had no effect on the localization of lamin B. We conclude that BAF is required for the assembly of emerin and A-type lamins at the reforming NE during telophase, and may mediate their stability in the subsequent interphase.
authors.affiliation: CREST Research Project of the Japan Science and Technology Corporation, Kansai Advanced Research Center, Communications Research Laboratory, 588-2 Iwaoka, Iwaoka-cho, Nishi-ku, Kobe 651-2492, Japan. tokuko@crl.go.jp
authors.forename: T
authors.initials: T
authors.lastname: Haraguchi
authors.forename: T
authors.initials: T
authors.lastname: Koujin
authors.forename: M
authors.initials: M
authors.lastname: Segura-Totten
authors.forename: K K
authors.initials: KK
authors.lastname: Lee
authors.forename: Y
authors.initials: Y
authors.lastname: Matsuoka
authors.forename: Y
authors.initials: Y
authors.lastname: Yoneda
authors.forename: K L
authors.initials: KL
authors.lastname: Wilson
authors.forename: Y
authors.initials: Y
authors.lastname: Hiraoka
mesh_terms: D000595:Amino Acid Sequence; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D006367:HeLa Cells; D006801:Humans; D034904:Lamin Type A; D034921:Lamin Type B; D034882:Lamins; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D020125:Mutation, Missense; D009685:Nuclear Envelope / Q000378:metabolism*; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism; D017434:Protein Structure, Tertiary / Q000235:genetics; D017384:Sequence Deletion; D013692:Telophase / Q000235:genetics; D013946:Thymopoietins / Q000235:genetics / Q000378:metabolism*
chemical_list: C501959:BANF1 protein, human; D004268:DNA-Binding Proteins; D034904:Lamin Type A; D034921:Lamin Type B; D034882:Lamins; D008565:Membrane Proteins; D009687:Nuclear Proteins; D013946:Thymopoietins; C092710:emerin; C093413:lamina-associated polypeptide 2