E3 ubiquitin-protein ligase CBL-C (CBLC)

E3 ubiquitin-protein ligase CBL-C (CBLC) is a member of the Cbl family of E3 ubiquitin ligases that functions as a regulator of cell signaling by ubiquitinating and promoting the degradation of activated receptor tyrosine kinases, such as EGFR and RET[1][2]. CBLC is involved in downregulation of signaling pathways critical for cell proliferation and differentiation, and its expression is mainly detected in epithelial cells. CBLC has been associated with modulation of cellular processes relevant to cancer biology, including proliferation and metastasis, and pathogenic variants are linked to disorders such as thrombocythemia and myeloproliferative neoplasms[1][3]. CBLC acts through recognition of phosphorylated targets and collaborates with E2 ubiquitin-conjugating enzymes to tag targets for proteasomal degradation, with a documented role in limiting EGFR and RET signaling[1].

Other names

Cbl proto-oncogene CRNF57CBL-3CBL-SLCas-Br-M (murine) ecotropic retroviral transforming sequence cRING-type E3 ubiquitin transferase CBL-CSH3-binding protein CBL-Csignal transduction protein CBL-C

Ubiquitination and proteasomal degradation of specific phosphorylated proteins (e.g., receptor tyrosine kinases)