Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2000-7-17
pubmed:abstractText
The choice of sexual identity in Drosophila is determined by a system that measures the X chromosome to autosome ratio (X/A). This system depends upon unequal expression of X-linked numerator genes in 1X and 2X nuclei. The numerators activate a special Sxl promoter, Sxl-Pe, in 2X/2A nuclei, but not 1X/2A nuclei. By multimerizing a conserved Sxl-Pe sequence block, we generated a gain-of-function promoter, Sxl-PeGOF, that is inappropriately active in 1X/2A nuclei. GOF activity requires the X-linked unpaired (upd) gene, which encodes a ligand for the Drosophila JAK/STAT signaling pathway. upd also functions as a numerator element in regulating wild-type Sxl-Pe reporters. We demonstrate that the JAK kinase, Hopscotch, and the STAT DNA-binding protein, Marelle, are also required for Sxl-Pe activation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/JNK Mitogen-Activated Protein..., http://linkedlifedata.com/resource/pubmed/chemical/Janus Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Sxl protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/hopscotch protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/os protein, Drosophila
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1097-2765
pubmed:author
pubmed:issnType
Print
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
581-7
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:10882142-Amino Acid Sequence, pubmed-meshheading:10882142-Animals, pubmed-meshheading:10882142-Conserved Sequence, pubmed-meshheading:10882142-DNA-Binding Proteins, pubmed-meshheading:10882142-Drosophila Proteins, pubmed-meshheading:10882142-Drosophila melanogaster, pubmed-meshheading:10882142-Female, pubmed-meshheading:10882142-Glycoproteins, pubmed-meshheading:10882142-JNK Mitogen-Activated Protein Kinases, pubmed-meshheading:10882142-Janus Kinases, pubmed-meshheading:10882142-Mitogen-Activated Protein Kinases, pubmed-meshheading:10882142-Promoter Regions, Genetic, pubmed-meshheading:10882142-Protein Kinases, pubmed-meshheading:10882142-Protein-Tyrosine Kinases, pubmed-meshheading:10882142-RNA-Binding Proteins, pubmed-meshheading:10882142-Repetitive Sequences, Amino Acid, pubmed-meshheading:10882142-Sex Determination Processes, pubmed-meshheading:10882142-Signal Transduction, pubmed-meshheading:10882142-Trans-Activators, pubmed-meshheading:10882142-Transcription Factors
pubmed:year
2000
pubmed:articleTitle
The JAK/STAT signaling pathway is required for the initial choice of sexual identity in Drosophila melanogaster.
pubmed:affiliation
Department of Molecular Biology, Princeton University, New Jersey 08544, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.