A 70-KDa Protein Facilitates Interleukin-4 Signal Transduction in the Absence of the Common Gamma Receptor Chain

Interleukin-4 signal transduction (and activation of STAT 6) is known to be mediated via its binding to a p140 receptor chain and the common gamma chain (γc). In non-activated monocytes, neither the γc nor its associated signal transducing molecule, Jak3, is expressed. We nevertheless show that IL-4...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 1997-04, Vol.233 (1), p.279-282
Main Authors: Dawson, C.H., Brown, B.L., Dobson, P.R.M.
Format: Article
Language:English
Subjects:
Antigens, CD - metabolism
Cell Line
Humans
Interleukin-4 - metabolism
Janus Kinase 3
Phosphorylation
Protein-Tyrosine Kinases - metabolism
Receptors, Interleukin - metabolism
Receptors, Interleukin-4
Signal Transduction
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Summary:Interleukin-4 signal transduction (and activation of STAT 6) is known to be mediated via its binding to a p140 receptor chain and the common gamma chain (γc). In non-activated monocytes, neither the γc nor its associated signal transducing molecule, Jak3, is expressed. We nevertheless show that IL-4 can initiate the tyrosine phosphorylation and DNA binding of STAT 6 in these cells. We present evidence for an additional 70 kDa IL-4 receptor chain which mediates the tyrosine phosphorylation of STAT 6 via Jak2, and suggest that this is the means by which IL-4 can signal in cells lacking the γc.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1997.6397