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Neu differentiation factor (NDF, or heregulin) and epidermal
growth factor (EGF) are structurally related proteins that bind to
distinct members of the ErbB family of receptor tyrosine kinases. Here
we show that NDF inhibits EGF binding in a cell type-specific manner.
The inhibitory effect is distinct from previously characterized
mechanisms that involve protein kinase C and receptor internalization
because it occurred at 4 °C and displayed reversibility. The extent
of inhibition correlated with both receptor saturation and affinity of
different NDF isoforms, and it was abolished upon overexpression of
either EGF receptor or ErbB-2. Binding kinetics and equilibrium
analyses indicated that NDF reduced the affinity, rather than the
number, of EGF receptors, through an acceleration of the rate of ligand
dissociation and deceleration of the association rate. On the basis of
co-immunoprecipitation of EGF and NDF receptors, we attribute the
inhibitory effect to the formation of receptor heterodimers. According
to this model, EGF binding to NDF-occupied heterodimers is partially
blocked. This model of negative trans-regulation within the ErbB family
is relevant to other subgroups of receptor tyrosine kinases and may
have physiological implications.
Volume 270,
Number 17,
Issue of April 28, pp. 9982-9990, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
A MODEL FOR TRANS-REGULATION WITHIN THE ErbB FAMILY OF RECEPTOR
TYROSINE KINASES
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