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
|