title: MBLR, a new RING finger protein resembling mammalian Polycomb gene products, is regulated by cell cycle-dependent phosphorylation.
abstract: BACKGROUND
  The RING finger proteins function in a variety of fundamental cellular processes. The products of some members of the Polycomb group (PcG) bear ring finger domains and are defined as a subclass of RING finger proteins. Among them are Drosophila posterior sex combs and suppressor 2 of zeste, whose RING fingers are conserved in vertebrate PcG proteins Mel18 and Bmi1.
  
  
  RESULTS
  We have identified a new mammalian RING finger protein, termed MBLR due to its structural similarity to Mel18 and Bmi1 (Mel18 and Bmi1-like RING finger protein). MBLR interacts with some PcG proteins: in vitro biochemical data support the idea of a direct interaction of MBLR's RING finger domain with Ring1B, which is highly homologous to one of the mammalian PcG genes, Ring1A. We also show that MBLR acts as a transcriptional repressor in transiently transfected cells, as is the case for other PcG proteins. Immunocytochemical analysis reveals that MBLR protein is localized in a fine-grained distribution throughout the nucleoplasm in interphase cultured cells and in a fainter diffuse cytoplasmic distribution in mitotic cells. In addition, we find that serine 32 of MBLR is specifically phosphorylated during mitosis, most likely by CDK7, a component of the basal transcriptional machinery.
  
  
  CONCLUSIONS
  Similarities to previously defined PcG proteins suggest that MBLR should be included in the same subclass of RING finger proteins as Mel18 and Bmi1. Although the biological relevance of the cell cycle-related phosphorylation remains to be demonstrated, serine 32 phosphorylation could nevertheless be functionally important.
authors.affiliation: Department of Cellular, Molecular and Developmental Biology, University of Michigan, 830 N University, Ann Arbor, MI 48109-1048, USA. takasaka@umich.edu
authors.forename: Takeshi
authors.initials: T
authors.lastname: Akasaka
authors.forename: Naomi
authors.initials: N
authors.lastname: Takahashi
authors.forename: Maki
authors.initials: M
authors.lastname: Suzuki
authors.forename: Haruhiko
authors.initials: H
authors.lastname: Koseki
authors.forename: Rolf
authors.initials: R
authors.lastname: Bodmer
authors.forename: Hisashi
authors.initials: H
authors.lastname: Koga
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D002453:Cell Cycle; D002460:Cell Line; D003001:Cloning, Molecular; D018076:DNA, Complementary; D004622:Embryo, Mammalian / Q000378:metabolism; D018507:Gene Expression Regulation, Developmental; D006801:Humans; D017403:In Situ Hybridization; D051379:Mice; D008969:Molecular Sequence Data; D010766:Phosphorylation; D063150:Polycomb Repressive Complex 1; D063146:Polycomb-Group Proteins; D012097:Repressor Proteins / Q000737:chemistry / Q000235:genetics*; D017386:Sequence Homology, Amino Acid
chemical_list: D018076:DNA, Complementary; C472312:PCGF6 protein, human; C066476:Pcgf6 protein, mouse; D063146:Polycomb-Group Proteins; D012097:Repressor Proteins; D063150:Polycomb Repressive Complex 1