Abstract

Recently, a large new family of E3 ubiquitin ligases, CUL4-DDB1-based E3 ligases, was identified in Arabidopsis and rice, following the discovery of hundreds of DDB1-CUL4 Associated Factor (DCAF) proteins. Current evidence suggests that distinct DCAF proteins are physically connected via DDB1 with CUL4 to form individual E3 complexes in which DCAF proteins function as the substrate receptors mediating specific ubiquitination of target proteins in multiple biological processes. Further characterization of these DCAF proteins will help reveal the likely divergent biological functions of the new E3 ligases in this family.

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