[HTML][HTML] Dimerization of substrate adaptors can facilitate cullin-mediated ubiquitylation of proteins by a “tethering” mechanism: a two-site interaction model for the Nrf2 …
M McMahon, N Thomas, K Itoh, M Yamamoto… - Journal of Biological …, 2006 - ASBMB
The prevalence and mechanistic significance of self-association among substrate adaptors
for the Cul-Rbx family of ubiquitin ligases remain unclear. We now report that it is as a
homodimer that the substrate adaptor Keap1 interacts with Cul3. The resulting complex
facilitates ubiquitylation of the Nrf2 transcription factor but only when this substrate
possesses within its Neh2 domain a second cryptic Keap1-binding site, the DLG motif, in
addition to its previously described ETGE site. Both motifs recognize overlapping surfaces …
for the Cul-Rbx family of ubiquitin ligases remain unclear. We now report that it is as a
homodimer that the substrate adaptor Keap1 interacts with Cul3. The resulting complex
facilitates ubiquitylation of the Nrf2 transcription factor but only when this substrate
possesses within its Neh2 domain a second cryptic Keap1-binding site, the DLG motif, in
addition to its previously described ETGE site. Both motifs recognize overlapping surfaces …