{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD041666/Q20211108_05.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD041666/Q20210927_11.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD041666/Q20210927_13.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD041666/Q20211108_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD041666/Q20210927_09.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD041666/Q20211108_07.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD041666/Q20210927_05.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD041666/Q20210927_07.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD041666/Q20211108_09.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD041666/Q20210927_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD041666/Q20211108_13.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD041666/Q20211108_11.raw"],"Pepxml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD041666/Q20210927_07.pep.xml","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD041666/Q20211108_03.pep.xml","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD041666/Q20211108_11.pep.xml","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD041666/Q20210927_09.pep.xml","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD041666/Q20211108_05.pep.xml","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD041666/Q20210927_13.pep.xml","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD041666/Q20210927_05.pep.xml","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD041666/Q20211108_13.pep.xml","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD041666/Q20211108_09.pep.xml","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD041666/Q20211108_07.pep.xml","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD041666/Q20210927_03.pep.xml","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD041666/Q20210927_11.pep.xml"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["sxu@ciw.edu"],"submitter":["Shouling Xu"],"technology_type":["Mass Spectrometry","Shotgun proteomics"],"software":[""],"submitter_keywords":["Ctr1","Ethylene","Mass spectrometry","Turboid","Proximity labeling"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD041666"],"tissue":["Leaf"],"sample_protocol":["A total of four biological replicates for each of two samples (GFP-CTR1-Turbo andGFP-Turbo) were prepared in two individual experiments, with two replicates in each. The protein expression in N. benthamiana and biotin treatment were done with the leaf fragments being treated with 50 µM biotin for 120 minutes. After biotin treatment, 1 g of finely ground N. benthamiana leaf tissue was resuspended in 2 ml of ice-cold extraction buffer (50 mM Tris pH 7.5, 150 mM NaCl, 0.1 % SDS, 1 % Triton-X-100, 0.5 % Na-deoxycholate, 1 mM EGTA, 1 mM DTT, 1x complete protease inhibitor, and 1 mM PMSF), sonicated in an ice bath for 2 min (10 sec on/ 10 sec off). All subsequent steps were done on ice or at 4°C. The tissue suspensions were centrifuged at 1500 rpm for 5 min to remove debris. The supernatant was then centrifuged again at 12000 rpm for 10 min to remove further debris. The extracts were first desalted using a PD-10 desalting column to remove free biotin (Cytiva). Next, the protein extract was incubated overnight with a 200 µl bead slurry of MyOne Streptavidin C1 (Invitrogen), which was  pre-washed with an extraction buffer on a rotor wheel. The beads were washed with cold extraction buffer, equilibrium buffer (50 mM Tris pH 7.5, 150 mM NaCl, 0.1 % SDS, 1 % Triton-X-100, 0.5 % Na-deoxycholate, 1 mM EGTA, and 1 mM DTT), 1 M KCl, 100 mM Na2CO3, and 2 M urea in 10 mM Tris (pH 8) at room temperature and shipped to MS facility. For on-beads tryptic digestion, the streptavidin beads were washed with 1x cold 1 M KCl, 1x 2 M Urea in 10 mM Tris-HCl pH 8, 2x cold 50 mM Tris pH 7.5, 2x with Urea wash buffer 3 (50 mM Tris pH 7.5, 1 M Urea), followed by three hours of incubation in Trypsin buffer (50 mM Tris pH 7.5, 1 M Urea, 1m M DTT, 0.4 µg Trypsin) at 25°C. The supernatant from tryptic digest and two washes with 60 µl 1 M Urea in 50 mM Tris pH 7.5 were reduced, alkylated and digested overnight with 0.5 µg Trypsin. Another 0.5 ug of trypsin were added in the next morning followed by acidification four hours later by adding formic acid to a final concentration of ~ 1 % and desalting using OMIX C18 pipette tips (A57003100). LC-MS/MS was done on a Q-Exactive HF hybrid quadrupole-Orbitrap mass spectrometer (Thermo Fisher), equipped with an Easy LC 1200 UPLC liquid chromatography system (Thermo Fisher). Peptides were first trapped using a trapping column (Acclaim PepMap 100 C18 HPLC, 75μm particle size, 2 cm bed length), then separated using an analytical column (Acclaim PepMap 100 C18 HPLC (2 μm particle size, 25cm bed length) (Thermo Fisher). The flow rate was 300 nL/min and a 120-min gradient was used. Peptides were eluted by a gradient from 3 to 28 % solvent B (80 % acetonitrile, 0.1 % formic acid) over 100 minutes and from 28 to 44 % solvent B over 20 minutes, followed by a short wash at 90 % solvent B. Precursor scan was from mass-to-charge ratio (m/z) 375 to 1,600 and top 20 most intense multiply charged precursors were selection for fragmentation. Peptides were fragmented with higher-energy collision dissociation (HCD) with normalized collision energy (NCE) 27. Raw File nameSample nameBiological ReplicatesConstructQ20210927_03.rawTURBO_1Control 1GFP-TurboIDQ20210927_05.rawTURBO_2Control 2GFP-TurboIDQ20210927_11.rawgCTR1_1gCTR1_1GFP-CTR1-TurboIDQ20210927_13.rawgCTR1_2gCTR1_2GFP-CTR1-TurboIDQ20211108_03.rawTURBO_3Control 3GFP-TurboIDQ20211108_05.rawTURBO_4Control 3GFP-TurboIDQ20211108_11.rawgCTR1_3gCTR1_3GFP-CTR1-TurboIDQ20211108_13.rawgCTR1_4gCTR1_4GFP-CTR1-TurboID"],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Mass Spectrometry data was searched using MaxQuant for Label Free Quantification (LFQ) and Protein Prospector for peptide counting. A MaxQuant (ver. 1.6.2.10) search was executed using default parameters with the following changes: In Group-specific parameters Label-free quantification was enabled with “Fast LFQ” checked. In global parameters “Match between runs” were enabled. For Identification, Peptides were searched against the uniprot-proteome_UP000084051 protein database (Downloaded 10/06/21) obtained from Uniprot containing a total of 73,606 entries. The proteingroups.txt file output from MaxQuant was analyzed in Perseus (ver. 1.6.15.0). LFQ intensities were imported and filtered with the following features: removing ‘reverse = +’, ‘potential contaminant = +’ and ‘only identified by site = +’. Data was log2 transformed and rows that were not identified in at least three replicates of one sample group were removed. Missing values were imputed from normal distribution (width = 0.3, down shift = 1.8, total matrix mode).A Student's t-test was executed to examine protein groups with different intensities between the elute and control groups. The t-test settings were the following: ‘Permutation-based FDR’, ‘FDR=0.15’,S0=2, ‘Report q-value’, ‘Number of Randomizations=250’ and ‘-log10 p-value’.Data was searched using Protein Prospector (ver. v 6.2.1). The data was searched against the same database, UniProtKB.UP000084051_4097 protein database concatenated with randomized peptides to calculate FDR. Spectral Counts were used to analyze data."],"omics_type":["Proteomics"],"labhead":["Shouling Xu"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Carnegie MS facility"],"species":["Nicotiana Tabacum (common Tobacco)"],"publication":["10.1002/PMIC.202300212"],"submitter_mail":["sxu@ciw.edu"],"submitter_affiliation":["Carnegie Institution at Stanford"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Uncovering  the proximal proteome of CTR1 through TurboID-mediated proximity labeling","description":"Protein-protein interactions play a crucial role in driving cellular processes and enabling appropriate physiological responses in organisms. The plant hormone ethylene signaling pathway is complex and regulated by the spatiotemporal regulation of its signaling molecules. Constitutive Triple Response 1 (CTR1), a key negative regulator of the pathway, regulates the function of Ethylene-Insensitive 2 (EIN2), a positive regulator of ethylene signaling, at the endoplasmic reticulum (ER) through phosphorylation. Our recent study revealed that CTR1 can also translocate from the ER to the nucleus in response to ethylene and positively regulate ethylene responses by stabilizing EIN3. To gain further insights into the role of CTR1 in plants, we used TurboID proximity labeling and mass spectrometry to identify the proximal proteomes of CTR1 in Nicotiana benthamiana. The identified proximal proteins include known ethylene signaling components, as well as proteins involved in diverse cellular processes such as carbon metabolism, mRNA metabolism, and organelle biogenesis. Our study demonstrates the feasibility of proximity labeling using the N. benthamiana transient expression system and identifies the potential interactors of CTR1 in vivo, unveiling the potential role of CTR1 in a wide range of cellular 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