Drosophila Myc is oncogenic in mammalian cells and plays a role in the diminutive phenotype

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 94; no. 4; pp. 1235 - 1240
• Main Authors: Schreiber-Agus, N. (Albert Einstein College of Medicine, Bronx, NY.), Stein, D, Chen, K, Goltz, J.S, Stevens, L, DePinho, R.A
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences of the United States of America 18-02-1997; National Acad Sciences; National Academy of Sciences; The National Academy of Sciences of the USA
• Subjects: ADN; Amino Acid Sequence; Animals; ARN MENSAJERO; ARN MESSAGER; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors; Basic-Leucine Zipper Transcription Factors; Biological Sciences; Biology; Cancer; Cell Differentiation; Cell Transformation, Neoplastic - genetics; Cells, Cultured; CERDA (PELO); Complementary DNA; COMPOSICION QUIMICA; COMPOSITION CHIMIQUE; DESARROLLO EMBRIONARIO; Developmental biology; DEVELOPPEMENT EMBRYONNAIRE; DNA; DNA-Binding Proteins - metabolism; Drosophila; Drosophila - genetics; Drosophila - growth & development; DROSOPHILA MELANOGASTER; Embryos; EXPRESION GENICA; EXPRESSION DES GENES; FENOTIPOS; FIBROBLASTE; FIBROBLASTOS; Fibroblasts - cytology; Genes; Genes, myc; Helix-Loop-Helix Motifs; Insects; Mammalia; Mammals; Mitosis; Molecular Sequence Data; MUTANT; MUTANTES; ONCOGENICIDAD; ONCOGENICITE; Open reading frames; PHENOTYPE; Protein Binding; PROTEINAS AGLUTINANTES; PROTEINE DE LIAISON; Proteins; Proto-Oncogene Proteins c-myc - metabolism; RAT; RATA; RATON; Rats; RNA; SACCHAROMYCES CEREVISIAE; SECUENCIA NUCLEOTIDICA; Sequence Homology, Amino Acid; SEQUENCE NUCLEOTIDIQUE; SOIES; SOURIS; Tissue Distribution; Transcription Factors - metabolism; Transcriptional Activation; TRANSFORMACION GENETICA; TRANSFORMATION GENETIQUE; Vertebrates; Yeasts
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.94.4.1235

Biochemical and biological activities of Myc oncoproteins are highly dependent upon their association with another basic region helix-loop-helix/leucine zipper (bHLH/LZ) protein, Max. Our previous observation that the DNA-binding/dimerization region of Max is absolutely conserved throughout vertebrate evolution provided the basis for a yeast two-hybrid interaction screen that led to the isolation of the Drosophila Myc (dMyc1) protein. Structural conservation in regions of known functional significance is consistent with the ability of dMyc1 to interact with vertebrate Max, to transactivate gene expression in yeast cells, and to cooperate with activated H-RAS to effect the malignant transformation of primary mammalian cells. The ability of P-element-mediated ectopic expression of dmyc1 to reverse a subset of the phenotypic alterations associated with the diminutive mutation suggests that diminutive may correspond to dmyc1. This finding, along with the localization of dmyc1 expression to zones of high proliferative activity in the embryo, implicates dMyc1 as an integral regulator of Drosophila growth and development