Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1993-4-29
pubmed:abstractText
The maternally expressed Drosophila gene torso (tor) is a receptor tyrosine kinase that, when activated, initiates a signal transduction cascade that is responsible for the proper differentiation of the terminal, nonsegmented regions of the embryo. l(1)pole hole, the Drosophila raf-1 serine-threonine kinase homolog, and corkscrew, a tyrosine phosphatase, have been shown previously to function in this signal transduction pathway. We have identified other products in this pathway by carrying out a mutagenesis screen for dominant suppressors of a tor gain-of-function allele. More than 40 mutations, some of which fall into seven complementation groups, have been characterized genetically. Two of these correspond to mutations in ras-1 and Son of sevenless (Sos), which also function in the sevenless and EGF receptor (Der) tyrosine kinase pathways. The phenotypes of several other Su(tor) mutations suggest that they also function in other receptor tyrosine kinase-activated pathways at different times during Drosophila development.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Eye Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Insect Hormones, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Protein Sorting Signals, 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/Proto-Oncogene Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-raf, http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Epidermal Growth Factor, http://linkedlifedata.com/resource/pubmed/chemical/Receptor Protein-Tyrosine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Son of Sevenless Proteins, http://linkedlifedata.com/resource/pubmed/chemical/sev protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/torso protein, Drosophila
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0890-9369
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
633-46
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:8384582-Alleles, pubmed-meshheading:8384582-Animals, pubmed-meshheading:8384582-Cell Differentiation, pubmed-meshheading:8384582-Chromosome Mapping, pubmed-meshheading:8384582-Drosophila, pubmed-meshheading:8384582-Drosophila Proteins, pubmed-meshheading:8384582-Eye Proteins, pubmed-meshheading:8384582-Female, pubmed-meshheading:8384582-Genes, Insect, pubmed-meshheading:8384582-Genetic Complementation Test, pubmed-meshheading:8384582-Insect Hormones, pubmed-meshheading:8384582-Male, pubmed-meshheading:8384582-Membrane Glycoproteins, pubmed-meshheading:8384582-Membrane Proteins, pubmed-meshheading:8384582-Morphogenesis, pubmed-meshheading:8384582-Mutagenesis, Site-Directed, pubmed-meshheading:8384582-Protein Sorting Signals, pubmed-meshheading:8384582-Protein-Serine-Threonine Kinases, pubmed-meshheading:8384582-Protein-Tyrosine Kinases, pubmed-meshheading:8384582-Proto-Oncogene Proteins, pubmed-meshheading:8384582-Proto-Oncogene Proteins c-raf, pubmed-meshheading:8384582-Receptor, Epidermal Growth Factor, pubmed-meshheading:8384582-Receptor Protein-Tyrosine Kinases, pubmed-meshheading:8384582-Signal Transduction, pubmed-meshheading:8384582-Son of Sevenless Proteins, pubmed-meshheading:8384582-Substrate Specificity, pubmed-meshheading:8384582-Suppression, Genetic, pubmed-meshheading:8384582-Temperature
pubmed:year
1993
pubmed:articleTitle
Torso, a receptor tyrosine kinase required for embryonic pattern formation, shares substrates with the sevenless and EGF-R pathways in Drosophila.
pubmed:affiliation
G.W. Hooper Foundation, University of California, San Francisco 94143-0552.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't