The complex becomes more complex: protein-protein interactions of SnRK1 with DUF581 family proteins provide a framework for cell- and stimulus type-specific SnRK1 signaling in plants

Nietzsche, Madlen; Schießl, Ingrid; Börnke, Frederik

doi:10.3389/fpls.2014.00054

Cited by 73 publications

(76 citation statements)

References 48 publications

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“…We demonstrated previously that both Arabidopsis SnRK1 catalytic a-subunits and STKR1 interact in yeast and, thus, hypothesized that STKR1 could be involved in SnRK1 signaling in plants (Nietzsche et al, 2014). In this study, we show by independent methods that both Arabidopsis SnRK1 a-subunit isoforms interact with STKR1 also in planta.…”

Section: Discussionmentioning

confidence: 48%

“…BiFC assays show that the interaction occurs predominantly inside the plant cell nucleus, which is consistent with a proposed role of STKR1 in transcriptional regulation (Curaba et al, 2003;Chevalier et al, 2008;Perazza et al, 2011) and suggests a functional link between STKR1-mediated transcriptional regulation and SnRK1 signaling inside the nucleus. Previous data suggest that SnRK1 can be localized to the cytosol as well as to the nucleus in Arabidopsis and N. benthamiana (Gazzarrini et al, 2004;Bitrián et al, 2011) and that the binding of SnRK1 to nucleus-localized proteins can change the partitioning in favor of a nuclear localization of the kinase (Nietzsche et al, 2014). Along that line, the interaction of SnRK1 with other transcription factors, such as FUSCA3, IDD8, and PETAL LOSS, also has been shown to occur inside the plant cell nucleus (Tsai and Gazzarrini, 2012;Jeong et al, 2015;O'Brien et al, 2015).…”

Section: Discussionmentioning

confidence: 70%

“…We have shown previously that the Arabidopsis STKR1 protein binds to the two SnRK1 a-subunits, AKIN10 and AKIN11, in the yeast two-hybrid system (Nietzsche et al, 2014). In order to investigate whether this interaction also occurs in planta, a bimolecular fluorescence complementation (BiFC) experiment was conducted in which either AKIN10 or AKIN11 was fused to the N-terminal 173 amino acids of the Venus protein and coexpressed together with STKR1 fused to the C-terminal 155 residues of Venus in leaves of Nicotiana benthamiana.…”

Section: Stkr1 and Snrk1 Interact Inside The Plant Cell Nucleusmentioning

confidence: 99%

“…Recently, Mair et al (2015) identified the Arabidopsis transcription factor bZIP63 as a key regulator of the starvation response and a direct target of the SnRK1 kinase. Phosphorylation of bZIP63 by SnRK1 was shown to change its dimerization preference, thereby affecting target gene expression and, ultimately, primary metabolism (Mair et al, 2015).In previous work, we established an Arabidopsis protein-protein interaction network around the two catalytic SnRK1 a-subunits, KIN10 and KIN11, that contains indirect and direct interactions of SnRK1 with a range of transcriptional regulators (Nietzsche et al, 2014(Nietzsche et al, , 2016. One protein found to interact with both SnRK1 a-subunits in yeast was STOREKEEPER RE-LATED1 (STKR1), also known as GL1 enhancer binding protein (GeBP; At4g00270.1; Curaba et al, 2003).…”

mentioning

confidence: 99%

“…In previous work, we established an Arabidopsis protein-protein interaction network around the two catalytic SnRK1 a-subunits, KIN10 and KIN11, that contains indirect and direct interactions of SnRK1 with a range of transcriptional regulators (Nietzsche et al, 2014(Nietzsche et al, , 2016. One protein found to interact with both SnRK1 a-subunits in yeast was STOREKEEPER RE-LATED1 (STKR1), also known as GL1 enhancer binding protein (GeBP; At4g00270.1; Curaba et al, 2003).…”

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confidence: 99%

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STOREKEEPER RELATED1/G-Element Binding Protein (STKR1) Interacts with Protein Kinase SnRK1

et al. 2017

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Sucrose nonfermenting related kinase1 (SnRK1) is a conserved energy sensor kinase that regulates cellular adaptation to energy deficit in plants. Activation of SnRK1 leads to the down-regulation of ATP-consuming biosynthetic processes and the stimulation of energy-generating catabolic reactions by transcriptional reprogramming and posttranslational modifications. Although considerable progress has been made during the last years in understanding the SnRK1 signaling pathway, many of its components remain unidentified. Here, we show that the catalytic a-subunits KIN10 and KIN11 of the Arabidopsis (Arabidopsis thaliana) SnRK1 complex interact with the STOREKEEPER RELATED1/G-Element Binding Protein (STKR1) inside the plant cell nucleus. Overexpression of STKR1 in transgenic Arabidopsis plants led to reduced growth, a delay in flowering, and strongly attenuated senescence. Metabolite profiling revealed that the transgenic lines exhausted their carbohydrates during the dark period to a greater extent than the wild type and accumulated a range of amino acids. At the global transcriptome level, genes affected by STKR1 overexpression were broadly associated with systemic acquired resistance, and transgenic plants showed enhanced resistance toward a virulent strain of the biotrophic oomycete pathogen Hyaloperonospora arabidopsidis Noco2. We discuss a possible connection of STKR1 function, SnRK1 signaling, and plant immunity.Plants are the prime example of photoautotrophic organisms, using photosynthesis to harness energy from sunlight for the conversion of CO 2 into energyrich carbohydrates. These photoassimilates are then directed to fuel plant growth and development. However, as sessile organisms, plants usually have to cope with strongly fluctuating environmental conditions, many of which negatively impact on energy availability, as they interfere with the production or distribution of photoassimilates. In order to maintain energy homeostasis and to promote survival, energy shortage triggers a massive cellular reprogramming characterized by nutrient remobilization, suppression of biosynthetic processes, and growth arrest (Baena-González, 2010). A central component of low-energy signaling in plants is the sucrose nonfermenting related kinase1 (SnRK1), which is orthologous to the AMP-dependent kinase (AMPK) and sucrose nonfermenting1 (SNF1) in mammals and yeast, respectively. Similar to its opisthokont counterparts, the SnRK1 holoenzyme is a heterotrimeric complex consisting of a catalytic a-subunit and noncatalytic b-and plant-specific bg-subunits (Ramon et al., 2013;Emanuelle et al., 2015). In Arabidopsis (Arabidopsis thaliana), the catalytic a-subunit is represented by two isoforms, SnRK1a1 (AKIN10; At3g01090) and SnRK1a2 (AKIN11; At3g29160), both of which appear to be expressed ubiquitously, although KIN10 accounts for the majority of SnRK1 activity (Jossier et al., 2009). Activation of SnRK1 involves the phosphorylation/ dephosphorylation of a T-loop Thr (Thr-172 of Arabidopsis SnRK1.1a) involving the upstream kinas...

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Section: Discussionmentioning

confidence: 48%

Section: Discussionmentioning

confidence: 70%

Section: Stkr1 and Snrk1 Interact Inside The Plant Cell Nucleusmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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STOREKEEPER RELATED1/G-Element Binding Protein (STKR1) Interacts with Protein Kinase SnRK1

et al. 2017

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Plant SnRK1 Kinases: Structure, Regulation, and Function

Margalha

Valerio

Baena-González

2016

Experientia Supplementum

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SnRK1 is an evolutionarily conserved protein kinase complex that regulates energy homeostasis in plants. In doing so, it promotes tolerance to adverse environmental conditions and influences a large array of growth and developmental processes. SnRK1 shares clear structural and functional similarities with its orthologs, yeast SNF1 and mammalian AMPK, but has evolved unique features that presumably provide a better adaptation to an autotrophic lifestyle. In this chapter, we review current knowledge on SnRK1, an atypical member of the SNF1/AMPK family, providing insight into its structure, regulation, and functions.

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