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J Biol Chem, Vol. 273, Issue 10, 5439-5442, March 6, 1998
From The Diabetes Unit and Medical Services and the Department of
Medicine, Harvard Medical School, Massachusetts General Hospital East,
Charlestown, Massachusetts 02129
The small GTP-binding protein Ras is pivotal in
transmitting growth and differentiation signals downstream of cell
surface receptors. Many observations have indicated that Ras transmits signals from cell surface receptors into multiple pathways via direct
interaction with different effectors in mammalian cells. We have
identified a novel potential Ras effector or target named Nore1. Nore1
has no significant sequence similarity to known mammalian proteins and
lacks an identifiable catalytic domain, but contains sequence motifs
that predict DAG_PE binding and SH3 domain binding. We show that Nore1
directly interacts with Ras in vitro in a
GTP-dependent manner, and the interaction requires an
intact Ras effector domain. Nore1 becomes associated with Ras in
situ following activation of epidermal growth factor receptor in
COS-7 and in KB cells.
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