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Mass spectrometric analysis of the endogenous type I interleukin-1 (IL-1) receptor signaling complex formed after IL-1 binding identifies IL-1RAcP, MyD88, and IRAK-4 as the stable components.

Abstract:

We investigated the composition of the endogenous ligand-bound type I interleukin-1 (IL-1) receptor (IL-1RI) signaling complex using immunoprecipitation and tandem mass spectrometry. Three proteins with approximate molecular masses of 60 (p60), 36 (p36), and 90 kDa (p90) became phosphorylated after treatment with IL-1. Phosphorylation in vitro of p60 has been reported previously, but its identity was unknown. We showed using tandem mass spectrometry that p60 is identical to interleukin-1 rece...

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Publication status:
Published

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Publisher copy:
10.1074/mcp.m600455-mcp200

Authors


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Institution:
University of Oxford
Department:
Oxford, MSD, NDORMS
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, NDORMS
Role:
Author
Journal:
Molecular and cellular proteomics : MCP
Volume:
6
Issue:
9
Pages:
1551-1559
Publication date:
2007-09-05
DOI:
EISSN:
1535-9484
ISSN:
1535-9476
URN:
uuid:6771ef80-6057-496f-85a9-ee557a77009a
Source identifiers:
226400
Local pid:
pubs:226400

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