lin-8, which antagonizes Caenorhabditis elegans Ras-mediated vulval induction, encodes a novel nuclear protein that interacts with the LIN-35 Rb protein
Program in Gene Function and Expression; Program in Molecular Medicine
Amino Acid Sequence; Animals; Caenorhabditis elegans; Caenorhabditis elegans Proteins; Female; Molecular Sequence Data; Nuclear Proteins; Repressor Proteins; Vulva; ras Proteins
Genetics and Genomics
Ras-mediated vulval development in C. elegans is inhibited by the functionally redundant sets of class A, B, and C synthetic Multivulva (synMuv) genes. Three of the class B synMuv genes encode an Rb/DP/E2F complex that, by analogy with its mammalian and Drosophila counterparts, has been proposed to silence genes required for vulval specification through chromatin modification and remodeling. Two class A synMuv genes, lin-15A and lin-56, encode novel nuclear proteins that appear to function as a complex. We show that a third class A synMuv gene, lin-8, is the defining member of a novel C. elegans gene family. The LIN-8 protein is nuclear and can interact physically with the product of the class B synMuv gene lin-35, the C. elegans homolog of mammalian Rb. LIN-8 likely acts with the synMuv A proteins LIN-15A and LIN-56 in the nucleus, possibly in a protein complex with the synMuv B protein LIN-35 Rb. Other LIN-8 family members may function in similar complexes in different cells or at different stages. The nuclear localization of LIN-15A, LIN-56, and LIN-8, as well as our observation of a direct physical interaction between class A and class B synMuv proteins, supports the hypothesis that the class A synMuv genes control vulval induction through the transcriptional regulation of gene expression.
DOI of Published Version
Genetics. 2005 Nov;171(3):1017-31. Epub 2005 Jul 14. Link to article on publisher's site
Davison, Ewa M.; Harrison, Melissa M.; Walhout, Albertha J. M.; Vidal, Marc; and Horvitz, H. Robert, "lin-8, which antagonizes Caenorhabditis elegans Ras-mediated vulval induction, encodes a novel nuclear protein that interacts with the LIN-35 Rb protein" (2005). Program in Gene Function and Expression Publications and Presentations. 22.