You are currently viewing the abstract.
View Full TextLog in to view the full text
AAAS login provides access to Science for AAAS members, and access to other journals in the Science family to users who have purchased individual subscriptions.
More options
Download and print this article for your personal scholarly, research, and educational use.
Buy a single issue of Science for just $15 USD.
Abstract
The Cbl proteins compose a family of ubiquitin ligases that play a central role in the down-regulation of signaling cascades involving receptor and nonreceptor tyrosine kinases. Analysis of the activity of these proteins suggests that they can regulate the signaling process through ubiquitination of the plasma membrane receptors and various downstream signaling components, including the Cbl proteins themselves. Structural analysis of the Cbl proteins shows that, in many instances, they interact with phosphorylated tyrosine residues on their targets. Furthermore, phosphorylation of specific tyrosine residues on the Cbl proteins may provide an additional level of control on the ubiquitinating activity of these proteins.