Recent Advances in Ubiquitin Signals Regulating Plant Membrane Trafficking.

Abstract

Ubiquitination is a reversible post-translational modification involving the attachment of ubiquitin, a 76-amino acid protein conserved among eukaryotes. The protein 'ubiquitin' was named after it was found to be ubiquitously expressed in cells. Ubiquitination was first identified as a post-translational modification that mediates energy-consuming protein degradation by the proteasome. After half a century, the manifold functions of ubiquitin are widely recognized to play key roles in diverse molecular pathways and physiological processes. Compared to humans, the number of enzymes related to ubiquitination is almost twice as high in plant species, such as Arabidopsis and rice, suggesting that this modification plays a critical role in many aspects of plant physiology including development and environmental stress responses. Here, we summarize and discuss recent knowledge of ubiquitination focusing on the regulation of membrane trafficking in plants. Ubiquitination of plasma membrane-localized proteins often leads to endocytosis and vacuolar targeting. In addition to cargo proteins, ubiquitination of membrane trafficking regulators regulates the morphodynamics of the endomembrane system. Thus, throughout this review, we focus on the physiological responses regulated by ubiquitination and their underlying mechanisms to clarify what is already known and what would be interesting to investigate in the future.