Autophagy is a major pathway that recycles cellular components in eukaryotic cells both under stressed and non-stressed conditions. Sugars participate both metabolically and as signaling molecules in development and response to various environmental and nutritional conditions. It is therefore essential to maintain metabolic homeostasis of sugars during non-stressed conditions in cells, not only to provide energy, but also to ensure effective signaling when exposed to stress. In both plants and animals, autophagy is activated by the energy sensor SnRK1/AMPK and inhibited by TOR kinase. SnRK1/AMPK and TOR kinases are both important regulators of cellular metabolism and are controlled to a large extent by the availability of sugars and sugar-phosphates in plants whereas in animals AMP/ATP indirectly translate sugar status. In plants, during nutrient and sugar deficiency, SnRK1 is activated, and TOR is inhibited to allow activation of autophagy which in turn recycles cellular components in an attempt to provide stress relief. Autophagy is thus indirectly regulated by the nutrient/sugar status of cells, but also regulates the level of nutrients/sugars by recycling cellular components. In both plants and animals sugars such as trehalose induce autophagy and in animals this is independent of the TOR pathway. The glucose-activated G-protein signaling pathway has also been demonstrated to activate autophagy, although the exact mechanism is not completely clear. This mini-review will focus on the interplay between sugar signaling and autophagy.

Naturally derived molecules can be used as priming or defense stimulatory agents to protect against biotic stress. Fructans have gained strong interest due to their ability to induce resistance in a number of crop species. In this study, we set out to establish the role of fructan-induced immunity against the fungal pathogen Botrytis cinerea in Arabidopsis thaliana. We show that both inulin- and levan-type fructans from different sources can enhance Arabidopsis resistance against B. cinerea. We found that inulin from chicory roots and levan oligosaccharides from the exopolysaccharide-producing bacterium Halomonas smyrnensis primed the NADPH-oxidase-mediated reactive oxygen species (ROS) burst in response to the elicitors flg22, derived from the bacterial flagellum, and oligogalacturonides (OGs), derived from the host cell wall. Neither induced a direct ROS burst typical of elicitors. We also found a primed response after infection with B. cinerea for H2O2 accumulation and the activities of ascorbate peroxidase and catalase. Sucrose accumulated as a consequence of fructan priming, and glucose and sucrose levels increased in fructan-treated plants after infection with B. cinerea. This study shows that levan-type fructans, specifically from bacterial origin, can prime plant defenses and that both inulin and levan oligosaccharide-mediated priming is associated with changes in ROS dynamics and sugar metabolism. Establishing fructan-induced immunity in Arabidopsis is an important step to further study the underlying mechanisms since a broad range of biological resources are available for Arabidopsis.

This perspective paper focuses on the most recent results suggesting a potential role for UDP-Glucose as a signaling molecule in plants. In animals, UDP-Glucose is well-established as an extracellular signaling molecule that is sensed by G-protein coupled receptors, activating several downstream defense mechanisms. Recent studies have shown that abnormal growth occurred in both vegetative and reproductive tissue of plants with reduced UDP-Glucose levels, and this could be rescued by exogenous UDP-Glucose. In plants with increased biomass accumulation, the genes involved in UDP-Glucose production were up-regulated. However, excessive endogenous accumulation of UDP-Glucose induced programmed cell death (PCD), and this could also be obtained by exogenous UDP-Glucose application. Plants with decreased UDP-glucose were insensitive to pathogen induced PCD. We speculate that UDP-Glucose acts as an extracellular signaling molecule in plants, and that it may be perceived as a damage-associated molecular pattern.

Glycation can be defined as an array of non-enzymatic post-translational modifications of proteins formed by their interaction with reducing carbohydrates and carbonyl products of their degradation. Initial steps of this process rely on reducing sugars and result in the formation of early glycation products—Amadori and Heyns compounds via Schiff base intermediates, whereas their oxidative degradation or reactions of proteins with α-dicarbonyl compounds yield a heterogeneous group of advanced glycation end products (AGEs). These compounds accompany thermal processing of protein-containing foods and are known to impact on ageing, pathogenesis of diabetes mellitus and Alzheimer’s disease in mammals. Surprisingly, despite high tissue carbohydrate contents, glycation of plant proteins was addressed only recently and its physiological role in plants is still not understood. Therefore, here we summarize and critically discuss the first steps done in the field of plant protein glycation during the last decade. We consider the main features of plant glycated proteome and discuss them in the context of characteristic metabolic background. Further, we address the possible role of protein glycation in plants and consider its probable contribution to protein degradation, methylglyoxal and sugar signalling, as well as interplay with antioxidant defense.

Upon stress, a trade-off between plant growth and defense responses defines the capacity for survival. Stress can result in accumulation of misfolded proteins in the endoplasmic reticulum (ER) and other organelles. To cope with these proteotoxic effects, plants rely on the unfolded protein response (UPR). The involvement of reactive oxygen species (ROS), ethylene (ETH), and sugars, as well as their crosstalk, in general stress responses is well established, yet their role in UPR deserves further scrutiny. Here, a synopsis of current evidence for ROS-ETH-sugar crosstalk in UPR is discussed. We propose that this triad acts as a major signaling hub at the crossroads of survival and death, integrating information from ER, chloroplasts, and mitochondria, thereby facilitating a coordinated stress response. Coordinated Inter-Organelle Stress Responses Facilitate Plant SurvivalThe sessile nature of plants implies that they are inherently subject to changing environments. As such, they need to cope with a variety of (a)biotic stresses. These harmful conditions lead to a set of shared but also distinct responses that can include oxidative stress (see Glossary), osmotic or ionic imbalances, and changes in cellular components, all of which modify the physiological status. Growth and development are hindered under such conditions, either directly, for instance by oxidative damage of essential biomolecules, or indirectly, through reprogramming of energy metabolism. In particular, the functioning of chloroplasts and mitochondria, the 'powerhouses' of the cell, is disturbed upon stress. The associated changes in carbohydrate status and ultimately energy levels, affect growth, but probably also serve as important stress signals (Figure 1, Key Figure) [1]. As such, mitochondria and chloroplasts act as central hubs that integrate external and internal signals to coordinate growth [2-4].Importantly, stress perception and its downstream responses should be considered as contextdependent, and are influenced by the stress type, severity, and duration. Nevertheless, an integral aspect of stress is the accumulation of unfolded or misfolded proteins (i.e., proteotoxic stress) [5]. The ER is essential for protein folding and secretion and has different mechanisms for protein quality control (QC). However, once the amount of unfolded or misfolded proteins surpasses the level that can be controlled by the ERQC, cells have to cope with the cytotoxicity of hampered proteostasis, called ER stress. This also occurs in chloroplasts and mitochondria [6,7]. Restoration of organellar proteostasis requires responses from both the organelle and the nucleus, and depends on intricate crosstalk between subcellular compartments. Hence, a tight communication established via anterograde and retrograde signaling is necessary for coordinated gene expression to restore proteostasis (Box 1). Eukaryotes rely on the evolutionary conserved retrograde signaling pathway called the UPR, that initiates a series of transcriptional Highlights Proteotoxic stress, or the ...