CRA-Genomics Research Centre; Fiorenzuola D'Arda, Italy.
Plant Signal Behav. 2012 Sep 1;7(9):1155-7. doi: 10.4161/psb.21367. Epub 2012 Aug 17.
Plant cells regulate many cellular processes controlling the half-life of critical proteins through ubiquitination. Previously, we characterized two interacting RING-type E3 ubiquitin ligases of Triticum durum, TdRF1 and WVIP2. We revealed their role in tolerance to dehydration, and existing knowledge about their partners also indicated their involvement in the regulation of some aspects of plant development. Here we located WVIP2 in the regulation of the ABA signaling, based on sequence similarities. Further we acquired general evidence about the versatility of ubiquitination in plant cells. A protein can be target of different E3 ligases for a perfect tuning of its abundance as well as the same E3 ligase can ubiquitinate different and unrelated proteins, thus representing a cross-connections between different signaling pathways for a global coordination of cellular processes.
植物细胞通过泛素化来调节许多控制关键蛋白质半衰期的细胞过程。此前，我们鉴定了两个相互作用的 RING 型 E3 泛素连接酶，即小麦 TdRF1 和 WVIP2。我们揭示了它们在耐旱性方面的作用，而且关于它们的伙伴的现有知识也表明它们参与了植物发育的某些方面的调节。在这里，我们根据序列相似性将 WVIP2 定位在 ABA 信号调节中。此外，我们获得了泛素化在植物细胞中的多功能性的一般证据。一种蛋白质可以成为不同 E3 连接酶的靶标，以精确调节其丰度，并且同一个 E3 连接酶可以泛素化不同和不相关的蛋白质，从而代表不同信号通路之间的交叉连接，以实现细胞过程的全局协调。
