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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1997-3-11
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pubmed:abstractText |
The interleukin-3 (IL-3), granulocyte-macrophage colony-stimulating factor, and IL-5 receptor alpha chains are each composed of three extracellular domains, a transmembrane domain and a short intracellular region. Domains 2 and 3 constitute the cytokine receptor module (CRM), typical of the cytokine receptor superfamily; however, the function of the N-terminal domain is not known. We have investigated the functions of the N-terminal and C-terminal domains of the IL-3 receptor (IL-3R) alpha chain. We find that cells transfected with the receptor beta chain (h beta c) and a truncated IL-3R alpha that is devoid of the intracellular region fail to proliferate or to activate STAT5 in response to human IL-3, despite binding the IL-3 with affinity indistinguishable from that of full-length receptor. In addition, IL-3-induced phosphorylation of h beta c was not detected. Thus, the IL-3R alpha intracellular region does not contribute detectably to stabilization of the receptor/ligand complex, but is essential for signal propagation. In contrast, a truncated IL-3R alpha with the N-terminal domain deleted interacts functionally with the beta chain; mouse cells transfected with these receptor chains proliferate in response to human IL-3 and STAT5 transcription factor is activated. High- and low-affinity binding sites are retained, although the affinity for IL-3 is decreased 15-fold, indicating a significant role for the N-terminal domain in IL-3 binding.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0006-4971
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
89
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
842-52
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9028315-Amino Acid Sequence,
pubmed-meshheading:9028315-Animals,
pubmed-meshheading:9028315-Antibodies, Blocking,
pubmed-meshheading:9028315-Antibodies, Monoclonal,
pubmed-meshheading:9028315-COS Cells,
pubmed-meshheading:9028315-Cytoplasm,
pubmed-meshheading:9028315-Intracellular Fluid,
pubmed-meshheading:9028315-Mutagenesis,
pubmed-meshheading:9028315-Protein Binding,
pubmed-meshheading:9028315-Protein Structure, Tertiary,
pubmed-meshheading:9028315-Receptors, Interleukin-3,
pubmed-meshheading:9028315-Signal Transduction
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pubmed:year |
1997
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pubmed:articleTitle |
Roles of the N and C terminal domains of the interleukin-3 receptor alpha chain in receptor function.
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pubmed:affiliation |
Hanson Centre for Cancer Research, Adelaide, Australia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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