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ube2m-rbx1 neddylation-cullin-ring-ligase proteins f-box protein slimb/β-trcp nature portfolio permissions reprints privacy policy e2-dependent ubiquitin-protein ligase advertising social media enhanced t-cell signalling nature 356 nature 365 nature 396 nature 403 nature 395 nature antigen-sensing signaling apparatus jun nh2-terminal kinase cbl-b-mediated ubiquitination chaperone-mediated autophagy regulates e3 ubiquitin ligases e3 ubiquitin ligase promoting ligand-induced tcr author information authors dual-recombinant murine retrovirus c-cbl-deficient mice gene-mediated resistance response cell cycle progression personal data xenopus development anergic t-lymphocyte clones ubiquitin ligase activity scf ubiquitin-ligase ubiquitin-dependent degradation ring e3 proteins data protection permissions springerlink instant access author correspondence author declares iκbα-ubiquitin ligase u-box proteins development t-cell clones cbl promotes ubiquitination jnk protein kinases cell receptor occupancy n-mediated resistance t-cell activation proline-rich domain conserved domain alignments

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         description:E3 ubiquitin ligases have emerged as key molecular regulators of immune cell function. Three families of proteins with ubiquitin ligase activity have been described (the HECT, RING and U-box proteins), and each may be involved in the regulation of immune responses during infection by targeting specific inhibitory molecules for proteolytic destruction. Several HECT and RING E3 proteins have now also been linked to the induction and maintenance of immune self-tolerance: c-Cbl, Cbl-b, GRAIL, Itch and Nedd4 each negatively regulate T cell growth factor production and proliferation. This review will discuss the relationship between the ubiquitination of select components of the antigen-sensing signaling apparatus in T cells and the development and maintenance of the clonal anergy state.
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