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Publication : Identification of Nore1 as a potential Ras effector.

First Author  Vavvas D Year  1998
Journal  J Biol Chem Volume  273
Issue  10 Pages  5439-42
PubMed ID  9488663 Mgi Jnum  J:46202
Mgi Id  MGI:1197353 Doi  10.1074/jbc.273.10.5439
Citation  Vavvas D, et al. (1998) Identification of Nore1 as a potential Ras effector. J Biol Chem 273(10):5439-42
abstractText  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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