Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2003-2-12
pubmed:abstractText
Metamorphosis of the Drosophila brain involves pruning of many larval-specific dendrites and axons followed by outgrowth of adult-specific processes. From a genetic mosaic screen, we recovered two independent mutations that block neuronal remodeling in the mushroom bodies (MBs). These phenotypically indistinguishable mutations affect Baboon function, a Drosophila TGF-beta/activin type I receptor, and dSmad2, its downstream transcriptional effector. We also show that Punt and Wit, two type II receptors, act redundantly in this process. In addition, knocking out dActivin around the mid-third instar stage interferes with remodeling. Binding of the insect steroid hormone ecdysone to distinct ecdysone receptor isoforms induces different metamorphic responses in various larval tissues. Interestingly, expression of the ecdysone receptor B1 isoform (EcR-B1) is reduced in activin pathway mutants, and restoring EcR-B1 expression significantly rescues remodeling defects. We conclude that the Drosophila Activin signaling pathway mediates neuronal remodeling in part by regulating EcR-B1 expression.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Activin Receptors, Type I, http://linkedlifedata.com/resource/pubmed/chemical/Activin Receptors, Type II, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Steroid, http://linkedlifedata.com/resource/pubmed/chemical/Smad2 Protein, http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators, http://linkedlifedata.com/resource/pubmed/chemical/Transforming Growth Factor beta, http://linkedlifedata.com/resource/pubmed/chemical/ecdysone receptor, http://linkedlifedata.com/resource/pubmed/chemical/put protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/wit protein, Drosophila
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
112
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
303-15
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:12581521-Activin Receptors, Type I, pubmed-meshheading:12581521-Activin Receptors, Type II, pubmed-meshheading:12581521-Animals, pubmed-meshheading:12581521-Brain, pubmed-meshheading:12581521-Cell Differentiation, pubmed-meshheading:12581521-DNA-Binding Proteins, pubmed-meshheading:12581521-Drosophila, pubmed-meshheading:12581521-Drosophila Proteins, pubmed-meshheading:12581521-Female, pubmed-meshheading:12581521-Genes, Lethal, pubmed-meshheading:12581521-Larva, pubmed-meshheading:12581521-Male, pubmed-meshheading:12581521-Mushroom Bodies, pubmed-meshheading:12581521-Mutation, Missense, pubmed-meshheading:12581521-Neural Pathways, pubmed-meshheading:12581521-Neuronal Plasticity, pubmed-meshheading:12581521-Neurons, pubmed-meshheading:12581521-Protein Isoforms, pubmed-meshheading:12581521-Proteins, pubmed-meshheading:12581521-Receptors, Cell Surface, pubmed-meshheading:12581521-Receptors, Steroid, pubmed-meshheading:12581521-Signal Transduction, pubmed-meshheading:12581521-Smad2 Protein, pubmed-meshheading:12581521-Trans-Activators, pubmed-meshheading:12581521-Transforming Growth Factor beta
pubmed:year
2003
pubmed:articleTitle
TGF-beta signaling activates steroid hormone receptor expression during neuronal remodeling in the Drosophila brain.
pubmed:affiliation
Department of Cell and Structural Biology, University of Illinois, Urbana, IL 61801, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't