Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6414
pubmed:dateCreated
1993-3-29
pubmed:abstractText
The fate of the R7 photoreceptor cell in the Drosophila compound eye is established by a specific inductive interaction between the R8 photoreceptor neuron and the R7 precursor cell. This induction is mediated by two cell-surface proteins: the ligand, bride of sevenless (boss), and sevenless (sev), a tyrosine-kinase receptor. The structure of boss is unique for a ligand of a tyrosine-kinase receptor. It contains a large extracellular domain, seven transmembrane segments, and a carboxy-terminal cytoplasmic tail. Here we report that: (1) boss activates tyrosine phosphorylation of the sev receptor; (2) the seven transmembrane domain of boss is necessary for its function; and (3) a soluble form of boss acts as an antagonist of the sev receptor both in vivo and in vitro.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Eye Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Ligands, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Receptor Protein-Tyrosine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Peptide, http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine, http://linkedlifedata.com/resource/pubmed/chemical/boss protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/sev protein, Drosophila
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0028-0836
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
361
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
732-6
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:7680109-Animals, pubmed-meshheading:7680109-Antibodies, Monoclonal, pubmed-meshheading:7680109-Bacterial Proteins, pubmed-meshheading:7680109-Cell Line, pubmed-meshheading:7680109-Drosophila, pubmed-meshheading:7680109-Drosophila Proteins, pubmed-meshheading:7680109-Eye Proteins, pubmed-meshheading:7680109-Gene Expression, pubmed-meshheading:7680109-Kinetics, pubmed-meshheading:7680109-Ligands, pubmed-meshheading:7680109-Membrane Glycoproteins, pubmed-meshheading:7680109-Neurons, pubmed-meshheading:7680109-Phosphotyrosine, pubmed-meshheading:7680109-Photoreceptor Cells, pubmed-meshheading:7680109-Protein-Serine-Threonine Kinases, pubmed-meshheading:7680109-Protein-Tyrosine Kinases, pubmed-meshheading:7680109-Receptor Protein-Tyrosine Kinases, pubmed-meshheading:7680109-Receptors, Cell Surface, pubmed-meshheading:7680109-Receptors, Peptide, pubmed-meshheading:7680109-Transfection, pubmed-meshheading:7680109-Tyrosine
pubmed:year
1993
pubmed:articleTitle
Extracellular domain of the boss transmembrane ligand acts as an antagonist of the sev receptor.
pubmed:affiliation
Howard Hughes Medical Institute, Department of Biological Chemistry, University of California, Los Angeles 90024.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't