Subcellular dynamics and protein-protein interactions of plant sucrose transporters

Abstract

Although extensively studied for their role in long distance transport, plant sucrose transporters are active not only in the phloem but throughout the plant body. Sucrose transporters of the SUT family were first described to be plasma membrane-resident proteins, but recent investigations revealed that subcellular dynamics of these transporters were part of complex regulatory mechanisms. The yeast two-hybrid split-ubiquitin system, tandem-affinity purification, and bimolecular-fluorescence complementation aided in identification of a complex network of SUT-interacting proteins that led to answers to many open questions. We found, for example, interacting proteins localized to other subcellular compartments. Although sucrose transporters were assumed to be localized mainly on the plasma membrane, and the tonoplast in the case of SUT4, the interaction partners were not exclusively predicted to be plasma membrane proteins, but belonged to the extracellular space (cell wall), intracellular vesicles, the ER, tonoplast, nuclei, and peroxisomes, among other cellular compartments. A subset of the SUT-interacting proteins localized exclusively to plasmodesmata. We conclude that (transient) protein-protein interactions of integral membrane proteins help to sequester SUTs to subcellular compartments, such as membrane microdomains, with specific functions to enable subcellular transport and cell-to-cell trafficking via plasmodesmata. Identification of SNARE proteins (soluble N-ethylmaleimide-sensitive factor protein attachment protein receptors) and protein disulfide isomerases support the assumption that the protein-protein interaction plays an important role for the subcellular movement of sugar transporters. It becomes apparent that the interaction partners provide a substantial impact on how and where the transporter is localized or processed for either targeting to a specific cellular or extracellular location, or tagging for degradation or recycling. In this review, interacting proteins, as well as the role of oligomeric complex formation, post-translational modification, and stress responses are summarized for SUTs of higher plants.