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J Biol Chem, Vol. 273, Issue 32, 20525-20534, August 7, 1998
From the Department of Biology, Emory University, Atlanta, Georgia
30322 and The neuregulins are receptor tyrosine kinase
ligands that play a critical role in the development of the heart,
nervous system, and breast. Unlike many extracellular signaling
molecules, such as the neurotrophins, most neuregulins are synthesized
as transmembrane proteins. To determine the functions of the highly
conserved neuregulin cytoplasmic tail, a yeast two-hybrid screen was
performed to identify proteins that interact with the 157-amino acid
sequence common to the cytoplasmic tails of all transmembrane
neuregulin isoforms.
This screen revealed that the neuregulin cytoplasmic tail interacts
with the LIM domain region of the nonreceptor protein kinase LIM kinase
1 (LIMK1). Interaction between the neuregulin cytoplasmic tail and
full-length LIMK1 was demonstrated by in vitro binding and
co-immunoprecipitation assays. Transmembrane neuregulins with each of
the three known neuregulin cytoplasmic tail isoforms interacted with
LIMK1. In contrast, the cytoplasmic tail of TGF-
Transmembrane Neuregulins Interact with LIM Kinase 1, a
Cytoplasmic Protein Kinase Implicated in Development of Visuospatial
Cognition
, and Amgen Inc., Thousand Oaks, California 91320
did not interact
with LIMK1. In vivo, neuregulin and LIMK1 are co-localized
at the neuromuscular synapse, suggesting that LIMK1, like neuregulin,
may play a role in synapse formation and maintenance. To our knowledge,
LIMK1 is the first identified protein shown to interact with the
cytoplasmic tail of a receptor tyrosine kinase ligand.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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