One Lyn molecule is sufficient to initiate phosphorylation of aggregated high-affinity IgE receptors

Carla Wofsy, Becky M. Vonakis, Henry Metzger, Byron Goldstein

Research output: Contribution to journalArticle

Abstract

In response to antigenic stimuli, the multi-subunit immune recognition receptors become aggregated and then phosphorylated on their cytoplasmic tyrosines. For the clonotypic receptors of B and T cells and for Fc receptors such as the high-affinity receptor for IgE (FcεRI), a Src family kinase initiates this phosphorylation. We ask whether aggregation of the initiating kinase itself is required for signal transduction or whether, alternatively, a single associated kinase molecule can phosphorylate the receptors in an aggregate. We formulate the alternative molecular mechanisms mathematically and compare predictions with experimental findings on FcεRI-bearing cells expressing varying amounts of the transfected Src family kinase Lyn. The data are consistent with the requirement of only a single Lyn molecule per FcεRI aggregate to initiate signaling and are inconsistent with a mechanism requiring more than one Lyn molecule.

Original languageEnglish (US)
Pages (from-to)8615-8620
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume96
Issue number15
DOIs
StatePublished - Jul 20 1999
Externally publishedYes

ASJC Scopus subject areas

  • General

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