Linked Life Data

14645129

Source:http://linkedlifedata.com/resource/pubmed/id/14645129

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2003-12-18
pubmed:abstractText
Pulses of the steroid hormone ecdysone trigger the major developmental transitions in Drosophila, including molting and puparium formation. The ecdysone signal is transduced by the EcR/USP nuclear receptor heterodimer that binds to specific response elements in the genome and directly regulates target gene transcription. We describe a novel nuclear receptor interacting protein encoded by rigor mortis (rig) that is required for ecdysone responses during larval development. rig mutants display defects in molting, delayed larval development, larval lethality, duplicated mouth parts, and defects in puparium formation--phenotypes that resemble those seen in EcR, usp, E75A and betaFTZ-F1 mutants. Although the expression of these nuclear receptor genes is essentially normal in rig mutant larvae, the ecdysone-triggered switch in E74 isoform expression is defective. rig encodes a protein with multiple WD-40 repeats and an LXXLL motif, sequences that act as specific protein-protein interaction domains. Consistent with the presence of these elements and the lethal phenotypes of rig mutants, Rig protein interacts with several Drosophila nuclear receptors in GST pull-down experiments, including EcR, USP, DHR3, SVP and betaFTZ-F1. The ligand binding domain of betaFTZ-F1 is sufficient for this interaction, which can occur in an AF-2-independent manner. Antibody stains reveal that Rig protein is present in the brain and imaginal discs of second and third instar larvae, where it is restricted to the cytoplasm. In larval salivary gland and midgut cells, however, Rig shuttles between the cytoplasm and nucleus in a spatially and temporally regulated manner, at times that correlate with the major lethal phase of rig mutants and major switches in ecdysone-regulated gene expression. Taken together, these data indicate that rig exerts essential functions during larval development through gene-specific effects on ecdysone-regulated transcription, most likely as a cofactor for one or more nuclear receptors. Furthermore, the dynamic intracellular redistribution of Rig protein suggests that it may act to refine spatial and temporal responses to ecdysone during development.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0950-1991
pubmed:author
pubmed:issnType
Print
pubmed:volume
131
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
25-36
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:14645129-Amino Acid Sequence, pubmed-meshheading:14645129-Animals, pubmed-meshheading:14645129-Base Sequence, pubmed-meshheading:14645129-Blotting, Northern, pubmed-meshheading:14645129-Brain, pubmed-meshheading:14645129-Carrier Proteins, pubmed-meshheading:14645129-Cell Nucleus, pubmed-meshheading:14645129-DNA Primers, pubmed-meshheading:14645129-Dimerization, pubmed-meshheading:14645129-Drosophila Proteins, pubmed-meshheading:14645129-Drosophila melanogaster, pubmed-meshheading:14645129-Ecdysone, pubmed-meshheading:14645129-Gene Expression Regulation, Developmental, pubmed-meshheading:14645129-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:14645129-Larva, pubmed-meshheading:14645129-Molecular Sequence Data, pubmed-meshheading:14645129-Polymerase Chain Reaction, pubmed-meshheading:14645129-Protein Isoforms, pubmed-meshheading:14645129-Pupa, pubmed-meshheading:14645129-Receptors, Cytoplasmic and Nuclear, pubmed-meshheading:14645129-Signal Transduction
pubmed:year
2004
pubmed:articleTitle
rigor mortis encodes a novel nuclear receptor interacting protein required for ecdysone signaling during Drosophila larval development.
pubmed:affiliation
Howard Hughes Medical Institute, Department of Human Genetics, University of Utah School of Medicine, Salt Lake City, UT 84112-5331, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't