Interplay between ethylene, ETP1/ETP2 F-box proteins, and degradation of EIN2 triggers ethylene responses in <i>Arabidopsis</i>

Qiao, Hong; Chang, Katherine N.; Yazaki, Junshi; Ecker, Joseph R.

doi:10.1101/gad.1765709

Cited by 298 publications

(291 citation statements)

References 51 publications

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“…The rapid turnover of proteins in this pathway has been known for some time (44,45). This rapid degradation is needed to quickly slow the rate of ethylene synthesis after its peak (44), and the degradation process is actively regulated as a means of manipulating ethylene signaling in plants (46). We identified several translational initiation factors known to be responsible for initiation of programmed cell death triggered as a response to Pseudomonas syringae infection (At1g26630 FBR12) and in brassinosteroid signaling in plants (At2g46280 TRIP-1) as among the most rapidly degrading proteins.…”

Section: The Value Of Partial 15 N Labeling Over Other Choices For Stmentioning

confidence: 99%

Determining Degradation and Synthesis Rates of Arabidopsis Proteins Using the Kinetics of Progressive 15N Labeling of Two-dimensional Gel-separated Protein Spots

Li¹,

Nelson

Solheim

et al. 2012

Molecular & Cellular Proteomics

100

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The growth and development of plant tissues is associated with an ordered succession of cellular processes that are reflected in the appearance and disappearance of proteins. The control of the kinetics of protein turnover is central to how plants can rapidly and specifically alter protein abundance and thus molecular function in response to environmental or developmental cues. However, the processes of turnover are largely hidden during periods of apparent steady-state protein abundance, and even when proteins accumulate it is unclear whether enhanced synthesis or decreased degradation is responsible. We have used a The growth and development of plant tissues is associated with an ordered succession of cellular processes that are dictated by the appearance and disappearance of proteins and the transcripts that encode them (1-4). The ratio of the synthesis and degradation rates of these molecules, whether they are in quasi-steady state or are rapidly changing in abundance, defines both the net turnover rate and the abundance of each (5). The control of the kinetics of these processes is central to how plants can rapidly alter specific protein abundance and thus molecular function to respond to environmental or developmental cues.Genome wide analysis of Arabidopsis mRNA turnover rates has confirmed that knowledge of transcript decay rates can provide insights into diverse biological processes (6). For example, the number of introns and sequence elements in the 3Ј-untranslated region and subcellular localization of the encoded protein affect the turnover rate of transcripts in Arabidopsis (6). Analysis of plant proteome synthesis and degradation has lagged considerably from our understanding of these processes in the transcriptome.Many methods have been developed to measure protein turnover in other organisms. Some are direct measurements of endogenous proteins using isotope labeling methods including both radioactive and stable isotope labeling (5, 7-10), whereas others use stable or transient transgenic techniques and a range of tags and markers (11,12). The clearest advantage of isotope labeling approaches is that the tags are very subtle with little or no impact on cellular processes and allow the fully functional proteins being assessed to be produced and distributed within cells in a normal context. The advent of mass spectrometry as a key tool in proteomics has provided a means to use enrichment of the natural abundance of stable isotopes to provide mass rather than radio decay signals to track the synthesis of new proteins. The ratio between light and heavy isotopes and the degrees of enrichment provided by mass spectrometry provides a powerful means to measure synthesis and degradation rates of individual proteins (5, 13).Stable isotope labeling using individual amino acids (SILAC) 1 has proven highly successful in mammalian cell culture systems (14). SILAC has also been used to measure protein turnover in yeast but required the use of auxotrophic mutants (5). However, N-methyl-N-(tert-butyldimethylsilyl...

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Section: The Value Of Partial 15 N Labeling Over Other Choices For Stmentioning

confidence: 99%

Determining Degradation and Synthesis Rates of Arabidopsis Proteins Using the Kinetics of Progressive 15N Labeling of Two-dimensional Gel-separated Protein Spots

Li¹,

Nelson

Solheim

et al. 2012

Molecular & Cellular Proteomics

100

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“…Ethylene binding to the active site promotes autophosphorylation of the receptor (Moussatche and Klee, 2004;Bisson and Groth, 2010) and inactivation of the downstream kinase CONSTITUTIVE TRIPLE RESPONSE1 (CTR1; Kieber et al, 1993). Active CTR1 kinase phosphorylates ETHYLENE INSENSITIVE2 (EIN2; Ju et al, 2012), an ER-bound N-ramp protein (Alonso et al, 1999), which is subsequently targeted for proteasomal degradation by two F-box proteins, EIN2 TARGETING PROTEIN1 (ETP1) and ETP2 (Qiao et al, 2009). When ethylene is bound to its receptor, EIN2 is not phosphorylated and gets cleaved by an unknown protease (Qiao et al, 2012).…”

Section: Plantsmentioning

confidence: 99%

Ethylene Exerts Species-Specific and Age-Dependent Control of Photosynthesis

Ceusters

Poel

2018

Plant Physiol.

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31The volatile plant hormone ethylene plays a regulatory role in many developmental processes and in 32 biotic and abiotic stress responses. One of the under-explored actions of ethylene is its regulation of 33 photosynthesis and associated components such as stomatal conductance, chlorophyll content, light 34 reactions, carboxylation events, carbohydrate partitioning, and age-related senescence. In this 35 update, we summarize the current knowledge concerning the regulation of photosynthesis, focusing 36 on the model species Arabidopsis thaliana. We describe how ethylene directs photosynthesis in 37 juvenile non-senescing leaves and mature senescing leaves. Furthermore, we extend these insights 38 Plant Physiology Preview.

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“…The proteasome degrades a series of nucleus-specific proteins, such as transcriptional regulators. For example, the proteasome degrades nuclear proteins NPR1, EIN2, and JAZ, which are important components of the signaling cascades of the stress hormones salicylic acid, ethylene, and jasmonate, respectively (Chini et al, 2007;Thines et al, 2007;Qiao et al, 2009;Spoel et al, 2009). SylA might be produced to interfere in these pathways.…”

Section: Nuclear Accumulation Of Sylamentioning

confidence: 99%

Proteasome Activity Imaging and Profiling Characterizes Bacterial Effector Syringolin A

et al. 2010

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Syringolin A (SylA) is a nonribosomal cyclic peptide produced by the bacterial pathogen Pseudomonas syringae pv syringae that can inhibit the eukaryotic proteasome. The proteasome is a multisubunit proteolytic complex that resides in the nucleus and cytoplasm and contains three subunits with different catalytic activities: b1, b2, and b5. Here, we studied how SylA targets the plant proteasome in living cells using activity-based profiling and imaging. We further developed this technology by introducing new, more selective probes and establishing procedures of noninvasive imaging in living Arabidopsis (Arabidopsis thaliana) cells. These studies showed that SylA preferentially targets b2 and b5 of the plant proteasome in vitro and in vivo. Structure-activity analysis revealed that the dipeptide tail of SylA contributes to b2 specificity and identified a nonreactive SylA derivative that proved essential for imaging experiments. Interestingly, subcellular imaging with probes based on epoxomicin and SylA showed that SylA accumulates in the nucleus of the plant cell and suggests that SylA targets the nuclear proteasome. Furthermore, subcellular fractionation studies showed that SylA labels nuclear and cytoplasmic proteasomes. The selectivity of SylA for the catalytic subunits and subcellular compartments is discussed, and the subunit selectivity is explained by crystallographic data.

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Interplay between ethylene, ETP1/ETP2 F-box proteins, and degradation of EIN2 triggers ethylene responses in Arabidopsis

Cited by 298 publications

References 51 publications

Determining Degradation and Synthesis Rates of Arabidopsis Proteins Using the Kinetics of Progressive 15N Labeling of Two-dimensional Gel-separated Protein Spots

Determining Degradation and Synthesis Rates of Arabidopsis Proteins Using the Kinetics of Progressive 15N Labeling of Two-dimensional Gel-separated Protein Spots

Ethylene Exerts Species-Specific and Age-Dependent Control of Photosynthesis

Proteasome Activity Imaging and Profiling Characterizes Bacterial Effector Syringolin A

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