CRL3-Mediated Ubiquitination in Arabidopsis: Roles of BTB Proteins in Diverse Biological Processes
摘要
Among the three enzymes that participate sequentially in the ubiquitination process, E3 ubiquitin ligase functions as a determinant of substrate specificity. As a multimeric E3 ubiquitin ligase, the Cullin-RING E3 ubiquitin ligase (CRL) complex constitutes the largest family of E3s. Unlike CRL1 and CRL4, which utilize an adaptor and substrate receptor as the substrate recognition module, CRL3 utilizes only BTB/POZ domain-containing proteins (BTB proteins), which directly bind Cullin 3 (CUL3) without an additional adaptor, as the substrate recognition module. In Arabidopsis, more than 690 F-box proteins and 119 DCAF proteins have been reported as substrate receptors of CRL1 and CRL4, respectively. In contrast, only 80 BTB proteins have been identified in Arabidopsis. BTB proteins participate in diverse processes, including hormone signaling, biotic/abiotic stress response, development processes, and light signaling, thereby contributing to the multifunctionality of CRL3. In this review, we aim to deepen the understanding of CRL3-mediated ubiquitination in Arabidopsis. We describe how BTB proteins recognize substrates and regulate their activity and stability, summarizing the recent progress in their involvement in various biological events.