Mummy, A UDP-N-acetylglucosamine pyrophosphorylase, modulates DPP signaling in the embryonic epidermis of Drosophila

Autor: Katherine L. Bates, Kathryn M. Monroe, Gregory B. Humphreys, Danielle Shipley, Molly C. Jud, Anthea Letsou, Matthew Higley, Suzanne S. Kimball, Marie Clougherty Vrablik
Rok vydání: 2013
Předmět:
Embryo
Nonmammalian
Glycosylation
Time Factors
animal structures
MAP Kinase Signaling System
Molecular Sequence Data
Embryonic Development
Context (language use)
Bone morphogenetic protein
Article
Gene product
03 medical and health sciences
0302 clinical medicine
Animals
Drosophila Proteins
Dorsal closure
Amino Acid Sequence
Molecular Biology
JNK signaling
030304 developmental biology
Dpp/BMP/TGF-β signaling
0303 health sciences
Organisms
Genetically Modified
biology
Gene Expression Regulation
Developmental
Cell Biology
biology.organism_classification
Nucleotidyltransferases
Molecular biology
Protein Structure
Tertiary
BMPR2
Enzyme Activation
Transcription Factor AP-1
Drosophila melanogaster
Bone Morphogenetic Proteins
embryonic structures
Phosphorylation
Epidermis
Raw
Signal transduction
030217 neurology & neurosurgery
Developmental Biology
Zdroj: Developmental Biology. 381(2):434-445
ISSN: 0012-1606
DOI: 10.1016/j.ydbio.2013.06.006
Popis: The evolutionarily conserved JNK/AP-1 (Jun N-terminal kinase/activator protein 1) and BMP (Bone Morphogenetic Protein) signaling cascades are deployed hierarchically to regulate dorsal closure in the fruit fly Drosophila melanogaster. In this developmental context, the JNK/AP-1 signaling cascade transcriptionally activates BMP signaling in leading edge epidermal cells. Here we show that the mummy (mmy) gene product, which is required for dorsal closure, functions as a BMP signaling antagonist. Genetic and biochemical tests of Mmy's role as a BMP-antagonist indicate that its function is independent of AP-1, the transcriptional trigger of BMP signal transduction in leading edge cells. pMAD (phosphorylated Mothers Against Dpp) activity data show the mmy gene product to be a new type of epidermal BMP regulator – one which transforms a BMP ligand from a long- to a short-range signal. mmy codes for the single UDP-N-acetylglucosamine pyrophosphorylase in Drosophila, and its requirement for attenuating epidermal BMP signaling during dorsal closure points to a new role for glycosylation in defining a highly restricted BMP activity field in the fly. These findings add a new dimension to our understanding of mechanisms modulating the BMP signaling gradient.
Databáze: OpenAIRE
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