Arabidopsis 14-3-3 Proteins: Fascinating and Less Fascinating Aspects

Jaspert, Nina; Throm, Christian; Oecking, Claudia

doi:10.3389/fpls.2011.00096

Cited by 63 publications

(63 citation statements)

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“…INTRODUCTION 14-3-3 proteins (14-3-3s) are phosphopeptide-binding proteins, which are highly conserved across eukaryotic cells including animals, plants and yeast (Roberts, 2003;Aitken, 2006;Jaspert et al, 2011). In Arabidopsis, there are a total of thirteen 14-3-3 genes predicted to encode functional proteins (Chevalier et al, 2009;Paul et al, 2012).…”

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confidence: 99%

“…In Arabidopsis, there are a total of thirteen 14-3-3 genes predicted to encode functional proteins (Chevalier et al, 2009;Paul et al, 2012). Numerous studies have revealed that plant 14-3-3s participate in the regulation of diverse biological and physiological processes, including primary metabolism, stress response, membrane transport and signal transduction cascades (Chevalier et al, 2009;Jaspert et al, 2011;Paul et al, 2012;de Boer et al, 2013). 14-3-3s act through direct interactions with target proteins, including transcription factors, metabolic enzymes, signaling components and ion channel proteins (Kanamaru et al, 1999;Bai et al, 2007;Gampala et al, 2007;Ryu et al, 2007;Li et al, 2012;Yoon and Kieber, 2013;Catala et al, 2014).…”

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confidence: 99%

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14‐3‐3 protein mediates plant seed oil biosynthesis through interaction with AtWRI1

Kong

Mantyla

et al. 2016

The Plant Journal

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Summary Plant 14‐3‐3 proteins are phosphopeptide‐binding proteins, belonging to a large family of proteins involved in numerous physiological processes including primary metabolism, although knowledge about the function of 14‐3‐3s in plant lipid metabolism is sparse. WRINKLED1 (WRI1) is a key transcription factor that governs plant oil biosynthesis. At present, AtWRI1‐interacting partners remain largely unknown. Here, we show that 14‐3‐3 proteins are able to interact with AtWRI1, both in yeast and plant cells. Transient co‐expression of 14‐3‐3‐ and AtWRI1‐encoding cDNAs led to increased oil biosynthesis in Nicotiana benthamiana leaves. Stable transgenic plants overproducing a 14‐3‐3 protein also displayed increased seed oil content. Co‐production of a 14‐3‐3 protein with AtWRI1 enhanced the transcriptional activity of AtWRI1. The 14‐3‐3 protein was found to increase the stability of AtWRI1. A possible 14‐3‐3 binding motif was identified in one of the two AP2 domains of AtWRI1, which was also found to be critical for the interaction of AtWRI1 with an E3 ligase linker protein. Thus, we hypothesize a regulatory mechanism by which the binding of 14‐3‐3 to AtWRI1 interferes with the interaction of AtWRI1 and the E3 ligase, thereby protecting AtWRI1 from degradation. Taken together, our studies identified AtWRI1 as a client of 14‐3‐3 proteins and provide insights into a role of 14‐3‐3 in mediating plant oil biosynthesis.

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14‐3‐3 protein mediates plant seed oil biosynthesis through interaction with AtWRI1

Kong

Mantyla

et al. 2016

The Plant Journal

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“…Furthermore, 14-3-3 proteins interact with the tonoplast potassium channel, TPK1, and strongly activate potassium transport activity [36,37]. Recently, it has been suggested that 14-3-3 proteins bind to mineral transporters including Zn, Mg, and Ca transporters [38,39,40,41]. Therefore, 14-3-3 proteins may play a role in nutrient accumulation.…”

Section: Resultsmentioning

confidence: 99%

Quantitative Proteomic Analysis of the Response to Zinc, Magnesium, and Calcium Deficiency in Specific Cell Types of Arabidopsis Roots

et al. 2016

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The proteome profiles of specific cell types have recently been investigated using techniques such as fluorescence activated cell sorting and laser capture microdissection. However, quantitative proteomic analysis of specific cell types has not yet been performed. In this study, to investigate the response of the proteome to zinc, magnesium, and calcium deficiency in specific cell types of Arabidopsis thaliana roots, we performed isobaric tags for relative and absolute quantification (iTRAQ)-based quantitative proteomics using GFP-expressing protoplasts collected by fluorescence-activated cell sorting. Protoplasts were collected from the pGL2-GFPer and pMGP-GFPer marker lines for epidermis or inner cell lines (pericycle, endodermis, and cortex), respectively. To increase the number of proteins identified, iTRAQ-labeled peptides were separated into 24 fractions by OFFGFEL electrophoresis prior to high-performance liquid chromatography coupled with mass spectrometry analysis. Overall, 1039 and 737 proteins were identified and quantified in the epidermal and inner cell lines, respectively. Interestingly, the expression of many proteins was decreased in the epidermis by mineral deficiency, although a weaker effect was observed in inner cell lines such as the pericycle, endodermis, and cortex. Here, we report for the first time the quantitative proteomics of specific cell types in Arabidopsis roots.

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“…In the Arabidopsis genome, six genes that encode ACOs were identified in silico by Babula et al (2006). Recently, ACO2 and ACO4 proteins were found, which may interact with 14-3-3 proteins in a yeast two-hybrid system (Jaspert et al , 2011). Together with the present results, this indicates that 14-3-3 proteins may regulate the ethylene biosynthesis pathway by modulating ACS and ACO proteins.…”

Section: Discussionmentioning

confidence: 99%

A type III ACC synthase, ACS7, is involved in root gravitropism in Arabidopsis thaliana

Huang

Chang

Wang

et al. 2013

Journal of Experimental Botany

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Ethylene is an important plant hormone that regulates developmental processes in plants. The ethylene biosynthesis pathway is a highly regulated process at both the transcriptional and post-translational level. The transcriptional regulation of these ethylene biosynthesis genes is well known. However, post-translational modifications of the key ethylene biosynthesis enzyme 1-aminocyclopropane-1-carboxylate (ACC) synthase (ACS) are little understood. In vitro kinase assays were conducted on the type III ACS, AtACS7, fusion protein and peptides to determine whether the AtACS7 protein can be phosphorylated by calcium-dependent protein kinase (CDPK). AtACS7 was phosphorylated at Ser216, Thr296, and Ser299 by AtCDPK16 in vitro. To investigate further the function of the ACS7 gene in Arabidopsis, an acs7-1 loss-of-function mutant was isolated. The acs7-1 mutant exhibited less sensitivity to the inhibition of root gravitropism by treatment with the calcium chelator ethylene glycol tetraacetic acid (EGTA). Seedlings were treated with gradient concentrations of ACC. The results showed that a certain concentration of ethylene enhanced the gravity response. Moreover, the acs7-1 mutant was less sensitive to inhibition of the gravity response by treatment with the auxin polar transport inhibitor 1-naphthylphthalamic acid, but exogenous ACC application recovered root gravitropism. Altogether, the results indicate that AtACS7 is involved in root gravitropism in a calcium-dependent manner in Arabidopsis.

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Arabidopsis 14-3-3 Proteins: Fascinating and Less Fascinating Aspects

Cited by 63 publications

References 42 publications

14‐3‐3 protein mediates plant seed oil biosynthesis through interaction with AtWRI1

14‐3‐3 protein mediates plant seed oil biosynthesis through interaction with AtWRI1

Quantitative Proteomic Analysis of the Response to Zinc, Magnesium, and Calcium Deficiency in Specific Cell Types of Arabidopsis Roots

A type III ACC synthase, ACS7, is involved in root gravitropism in Arabidopsis thaliana

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