Linked Life Data

7541671

Source:http://linkedlifedata.com/resource/pubmed/id/7541671

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1995-8-15
pubmed:abstractText
The erythropoietin (Epo) receptor belongs to the cytokine receptor superfamily. Although the cytokine receptors do not possess a tyrosine kinase consensus sequence in the intracellular domain, rapid stimulation of a tyrosine kinase activity occurs after activation by the ligand. We and others have shown that Epo induces the tyrosine phosphorylation of its cognate receptor as well as phosphorylation of other proteins. In this report, we examined the role of the receptor tyrosine residues in signal transduction. Eight tyrosine residues are located within the intracellular domain of the murine Epo receptor. A single tyrosine residue is present in the region previously shown to be sufficient for proliferative signal transduction. This tyrosine (Tyr 343) was mutated to phenylalanine. Moreover, mutant receptors were also generated with either a tyrosine residue or a phenylalanine residue at position 343 and with a COOH terminal truncation that removed the 7 other tyrosine residues. Expression vectors carrying these mutated receptors were transfected into the interleukin-3-dependent murine cell line Ba/F3. Epo-induced growth was sustained efficiently by all these receptors, although receptors without any tyrosine residues conferred a significantly reduced mitogenic activity. Moreover, all receptors were able to mediate Epo-dependant accumulation of beta-globin mRNA. The mutated receptors all induced the tyrosine phosphorylation of several cellular proteins after Epo stimulation. However, the truncated receptors induced the phosphorylation of a reduced number of proteins, suggesting that phosphorylated tyrosines of the receptor could have a role in the recruitment either of a tyrosine kinase or of tyrosine kinase substrate proteins. The receptors were all able to mediate Epo-induced activation of phosphatidylinositol 3-kinase, although truncated receptors no longer bound phosphatidylinositol 3-kinase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-4971
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
86
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
598-606
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:7541671-Cell Differentiation, pubmed-meshheading:7541671-Cell Line, pubmed-meshheading:7541671-Enzyme Activation, pubmed-meshheading:7541671-Erythropoiesis, pubmed-meshheading:7541671-Erythropoietin, pubmed-meshheading:7541671-Gene Expression Regulation, pubmed-meshheading:7541671-Globins, pubmed-meshheading:7541671-Hematopoietic Stem Cells, pubmed-meshheading:7541671-Interleukin-3, pubmed-meshheading:7541671-Mutagenesis, Site-Directed, pubmed-meshheading:7541671-Phosphatidylinositol 3-Kinases, pubmed-meshheading:7541671-Phosphorylation, pubmed-meshheading:7541671-Phosphotransferases (Alcohol Group Acceptor), pubmed-meshheading:7541671-Phosphotyrosine, pubmed-meshheading:7541671-Protein Processing, Post-Translational, pubmed-meshheading:7541671-Protein-Tyrosine Kinases, pubmed-meshheading:7541671-Receptors, Erythropoietin, pubmed-meshheading:7541671-Recombinant Fusion Proteins, pubmed-meshheading:7541671-Sequence Deletion, pubmed-meshheading:7541671-Signal Transduction, pubmed-meshheading:7541671-Transfection, pubmed-meshheading:7541671-Tyrosine
pubmed:year
1995
pubmed:articleTitle
Tyrosine phosphorylation of the erythropoietin receptor: role for differentiation and mitogenic signal transduction.
pubmed:affiliation
Institut Cochin de Génétique Moléculaire (ICGM), Université René Descartes, Paris, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't