The E3 ubiquitin ligase WVIP2 highlights the versatility of protein ubiquitination

Abstract

Determining the half-life of proteins, ubiquitination plays a fundamental role in the regulation of cellular processes through the proteasome-mediated protein degradation. Main actors of this theme are the E3 ubiquitin ligases which specifically recruit the protein targets for ubiquitination.1 Further, ubiquitination enzymes can crosstalk, providing an additional layer of ubiquitin-dependent control on cellular activities.The ubiquitin proteasome system strongly impacts on the signaling pathways of abiotic stress tolerance, including those dependent by ABA.2 The control of the E3 ligases on stress response can be exerted through the suppression of stress signaling pathways during favorable growth conditions, the degradation of negative regulators of stress response upon stress exposition, or the attenuation of stress signaling pathways for further growth once environmental conditions have improved. In a previous paper we showed that WVIP2 3 and TdRF1 are two RING finger proteins of durum wheat (Triticum durum) with a demonstrated ubiquitin ligases activity. 4 The corresponding genes are stress responsive, both upregulated upon cold treatment and downregulated by ABA, and with contrasting behavior in response to dehydration, with TdRF1 upregulated and WVIP2 downregulated. Further, transient induced gene silencing experiments suggested a positive and negative effect for TdRF1 and WVIP2, respectively, on tolerance to dehydration in vitro.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.

Discovering consensus genomic regions in wheat for root-related traits by QTL meta-analysis

“…These proteins play a role in the signal pathway of abiotic stresses tolerance, such as dehydration. Moreover, they are also involved in the regulation of plant development 44 . Additionally, five peaks corresponded to F-box domains that are the protein subunit of E3 ubiquitin ligases involved in the responses to abiotic stresses 45 .…”