Breast cancer regulation by traffic and degradation of ErbB family

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ErbB2/ErbB3 heterodimer is expressed on many breast cancers, and the signals derived from the dimer plays significant roles on malignant phenotypes. In the present study, I analyzed how the heterodimer is degraded. Whereas ErbB2 was relatively stable, ErbB3 was continuously degraded by the proteasome and lysosomes. NRG1βstimulation induced proteasome-dependent degradation. Among several E3s tested, I identified Nrdp1 and two additional E3s that ubiquitinated ErbB3.Further, intracellular portion of ErbB3 comprizing of 100 aminoacids was required for the degradation, suggesting the possible ubiquitination target of ErbB3.