DREAM represses distinct targets by cooperating with different THAP domain proteins. 2021

Csenge Gal, and Francesco Nicola Carelli, and Alex Appert, and Chiara Cerrato, and Ni Huang, and Yan Dong, and Jane Murphy, and Andrea Frapporti, and Julie Ahringer
Wellcome Trust/Cancer Research UK Gurdon Institute and Department of Genetics, University of Cambridge, Cambridge, UK.

The DREAM (dimerization partner [DP], retinoblastoma [Rb]-like, E2F, and MuvB) complex controls cellular quiescence by repressing cell-cycle and other genes, but its mechanism of action is unclear. Here, we demonstrate that two C. elegans THAP domain proteins, LIN-15B and LIN-36, co-localize with DREAM and function by different mechanisms for repression of distinct sets of targets. LIN-36 represses classical cell-cycle targets by promoting DREAM binding and gene body enrichment of H2A.Z, and we find that DREAM subunit EFL-1/E2F is specific for LIN-36 targets. In contrast, LIN-15B represses germline-specific targets in the soma by facilitating H3K9me2 promoter marking. We further find that LIN-36 and LIN-15B differently regulate DREAM binding. In humans, THAP proteins have been implicated in cell-cycle regulation by poorly understood mechanisms. We propose that THAP domain proteins are key mediators of Rb/DREAM function.

UI MeSH Term Description Entries
D011401 Promoter Regions, Genetic DNA sequences which are recognized (directly or indirectly) and bound by a DNA-dependent RNA polymerase during the initiation of transcription. Highly conserved sequences within the promoter include the Pribnow box in bacteria and the TATA BOX in eukaryotes. rRNA Promoter,Early Promoters, Genetic,Late Promoters, Genetic,Middle Promoters, Genetic,Promoter Regions,Promoter, Genetic,Promotor Regions,Promotor, Genetic,Pseudopromoter, Genetic,Early Promoter, Genetic,Genetic Late Promoter,Genetic Middle Promoters,Genetic Promoter,Genetic Promoter Region,Genetic Promoter Regions,Genetic Promoters,Genetic Promotor,Genetic Promotors,Genetic Pseudopromoter,Genetic Pseudopromoters,Late Promoter, Genetic,Middle Promoter, Genetic,Promoter Region,Promoter Region, Genetic,Promoter, Genetic Early,Promoter, rRNA,Promoters, Genetic,Promoters, Genetic Middle,Promoters, rRNA,Promotor Region,Promotors, Genetic,Pseudopromoters, Genetic,Region, Genetic Promoter,Region, Promoter,Region, Promotor,Regions, Genetic Promoter,Regions, Promoter,Regions, Promotor,rRNA Promoters
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D005786 Gene Expression Regulation Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation. Gene Action Regulation,Regulation of Gene Expression,Expression Regulation, Gene,Regulation, Gene Action,Regulation, Gene Expression
D006657 Histones Small chromosomal proteins (approx 12-20 kD) possessing an open, unfolded structure and attached to the DNA in cell nuclei by ionic linkages. Classification into the various types (designated histone I, histone II, etc.) is based on the relative amounts of arginine and lysine in each. Histone,Histone H1,Histone H1(s),Histone H2a,Histone H2b,Histone H3,Histone H3.3,Histone H4,Histone H5,Histone H7
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D014157 Transcription Factors Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process. Transcription Factor,Factor, Transcription,Factors, Transcription
D016160 Retinoblastoma Protein Product of the retinoblastoma tumor suppressor gene. It is a nuclear phosphoprotein hypothesized to normally act as an inhibitor of cell proliferation. Rb protein is absent in retinoblastoma cell lines. It also has been shown to form complexes with the adenovirus E1A protein, the SV40 T antigen, and the human papilloma virus E7 protein. Rb Protein,Retinoblastoma Nuclear Phosphoprotein p105-Rb,p105-Rb Protein,Rb Gene Product,Rb1 Gene Product,Retinoblastoma Nuclear Phosphoprotein p105 Rb,p105 Rb Protein
D017173 Caenorhabditis elegans A species of nematode that is widely used in biological, biochemical, and genetic studies. Caenorhabditis elegan,elegan, Caenorhabditis
D050684 E2F Transcription Factors A family of basic helix-loop-helix transcription factors that control expression of a variety of GENES involved in CELL CYCLE regulation. E2F transcription factors typically form heterodimeric complexes with TRANSCRIPTION FACTOR DP1 or transcription factor DP2, and they have N-terminal DNA binding and dimerization domains. E2F transcription factors can act as mediators of transcriptional repression or transcriptional activation. E2F Transcription Factor,E2F Proteins,Transcription Factor E2F,E2F, Transcription Factor,Factor, E2F Transcription,Transcription Factor, E2F,Transcription Factors, E2F
D054730 Protein Interaction Domains and Motifs Protein modules with conserved ligand-binding surfaces which mediate specific interaction functions in SIGNAL TRANSDUCTION PATHWAYS and the specific BINDING SITES of their cognate protein LIGANDS. Protein Interaction Domains,Protein Interaction Motifs,Binding Motifs, Protein Interaction,Protein Interaction Binding Motifs,Protein-Protein Interaction Domains,Domain, Protein Interaction,Domain, Protein-Protein Interaction,Domains, Protein Interaction,Domains, Protein-Protein Interaction,Motif, Protein Interaction,Motifs, Protein Interaction,Protein Interaction Domain,Protein Interaction Motif,Protein Protein Interaction Domains,Protein-Protein Interaction Domain

Related Publications

Csenge Gal, and Francesco Nicola Carelli, and Alex Appert, and Chiara Cerrato, and Ni Huang, and Yan Dong, and Jane Murphy, and Andrea Frapporti, and Julie Ahringer
January 1995, Current biology : CB,
Csenge Gal, and Francesco Nicola Carelli, and Alex Appert, and Chiara Cerrato, and Ni Huang, and Yan Dong, and Jane Murphy, and Andrea Frapporti, and Julie Ahringer
May 1999, Human molecular genetics,
Csenge Gal, and Francesco Nicola Carelli, and Alex Appert, and Chiara Cerrato, and Ni Huang, and Yan Dong, and Jane Murphy, and Andrea Frapporti, and Julie Ahringer
December 2018, Cell reports,
Csenge Gal, and Francesco Nicola Carelli, and Alex Appert, and Chiara Cerrato, and Ni Huang, and Yan Dong, and Jane Murphy, and Andrea Frapporti, and Julie Ahringer
November 2021, The New phytologist,
Csenge Gal, and Francesco Nicola Carelli, and Alex Appert, and Chiara Cerrato, and Ni Huang, and Yan Dong, and Jane Murphy, and Andrea Frapporti, and Julie Ahringer
April 2016, Epigenomics,
Csenge Gal, and Francesco Nicola Carelli, and Alex Appert, and Chiara Cerrato, and Ni Huang, and Yan Dong, and Jane Murphy, and Andrea Frapporti, and Julie Ahringer
February 2003, Trends in biochemical sciences,
Csenge Gal, and Francesco Nicola Carelli, and Alex Appert, and Chiara Cerrato, and Ni Huang, and Yan Dong, and Jane Murphy, and Andrea Frapporti, and Julie Ahringer
May 2013, Journal of biomolecular NMR,
Csenge Gal, and Francesco Nicola Carelli, and Alex Appert, and Chiara Cerrato, and Ni Huang, and Yan Dong, and Jane Murphy, and Andrea Frapporti, and Julie Ahringer
February 2023, Cerebral cortex (New York, N.Y. : 1991),
Csenge Gal, and Francesco Nicola Carelli, and Alex Appert, and Chiara Cerrato, and Ni Huang, and Yan Dong, and Jane Murphy, and Andrea Frapporti, and Julie Ahringer
March 2009, Journal of bacteriology,
Csenge Gal, and Francesco Nicola Carelli, and Alex Appert, and Chiara Cerrato, and Ni Huang, and Yan Dong, and Jane Murphy, and Andrea Frapporti, and Julie Ahringer
July 1990, Nature,
Copied contents to your clipboard!