Ubiquitination of lysine (K) residues in the cytoplasmic domain of cytokine receptors plays a major role in intracellular receptor routing and control of signal duration. However, which ubiquitin (E3) ligases and whether specific lysines, eg. present in conserved motifs, are involved in ubiquitin-mediated routing is still largely unknown. We recently showed that SOCS3, which forms an Elongin/Cullin-based E3 ligase (ECSSOCS3), is involved in ligand-induced ubiquitination, lysosomal routing and degradation of the G-CSFR (
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