{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065856/sample_information.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065856/proteinGroups_je5_vs_WT.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065856/E20230630_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065856/E20230727_06.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065856/E20230630_04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065856/E20231111_07.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065856/E20231111_04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065856/E20230823_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065856/E20231111_08.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065856/E20231111_06.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065856/E20231111_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065856/E20230727_05.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065856/E20230630_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065856/E20230727_04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065856/E20231111_03.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["sxu@ciw.edu"],"submitter":["Shouling Xu"],"technology_type":["Affinity purification coupled with mass spectrometry proteomics","Mass Spectrometry"],"software":[""],"submitter_keywords":["Ap-ms","Arabidopsis","Cesa3je5","Wild type (col-0)","Lti6b","Lc-ms/ms","Turboid"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD065856"],"tissue":["Seedling","Whole Body"],"sample_protocol":["Arabidopsis thaliana seeds of TbID-YFP-LTI6b/Col-0, Col-0, TbID-YFP-LTI6b/cesa3je5, and cesa3je5 were surface-sterilized using a solution of 30% bleach and 0.1% SDS for 20 minutes, followed by four rinses with sterile water. The sterilized seeds were stratified in the dark at 4°C for 2-3 days before being germinated on 1X Murashige and Skoog (MS) plates supplemented with 1% sucrose and solidified with 0.7% gelzan (pH 5.7). Seedlings were grown vertically in a growth chamber maintained at 22°C under a 16-hour light/8-hour dark photoperiod.  One gram of five-day-old whole seedlings grown on MS plates was harvested into a nylon biopsy bag (Fisher Scientific, catalog #50-303-41). The bag was submerged in 50 µM biotin in MS liquid medium for 15 minutes. After treatment, samples were washed with MS liquid and gently blotted on a paper towel to remove excess liquid. Samples were then flash-frozen in liquid nitrogen, ground into fine powder using a mortar and a pestle, and stored at -80°C for further use. One gram of the finely ground frozen tissue powder from the biotin treatment was resuspended in 2 mL of protein extraction buffer containing 50 mM Tris-HCl (pH 7.5), 150 mM NaCl, 0.1% SDS, 1% Triton X-100, 0.5% sodium deoxycholate, 1 mM EGTA, 1 mM DTT, 1× cOmplete protease inhibitor cocktail (Roche, catalog #COUEDTAF-RO), and 1 mM PMSF. The suspension was vortexed and incubated on a rotor wheel at 4°C for 10 min. Samples were then sonicated in an ice bath using a Branson 450 sonifier at 20% amplitude with 10 s on/10 s off pulses for a total of 2 min. Following sonication, samples were centrifuged at 12,000 g for 10 min at 4°C. A total of 2.5 mL of the resulting supernatant was loaded onto PD-10 desalting columns (Cytiva, catalog #17-0851-01) pre-equilibrated with equilibration buffer composed of 50 mM Tris-HCl (pH 7.5), 150 mM NaCl, 0.1% SDS, 1% Triton X-100, 0.5% sodium deoxycholate, 1 mM EGTA, and 1 mM DTT. Proteins were eluted with 3.5 mL of equilibration buffer into 5 mL LoBind tubes (Eppendorf, catalog #0030108302). For streptavidin pulldown, 200 µL of Dynabeads MyOne Streptavidin T1 beads (Thermo Fisher, catalog #65602) were washed with extraction buffer and then incubated with the desalted protein extract supplemented with 1× cOmplete protease inhibitor cocktail and 1 mM PMSF. The mixture was incubated overnight at 4°C on a rotor wheel. The following day, beads were separated using a magnetic rack, transferred to 1.5 mL LoBind tubes (Eppendorf, catalog #022431081), and subjected to a series of washes: twice with cold extraction buffer, twice with cold equilibration buffer, once with cold 1 M KCl, transferred to a fresh 1.5 mL LoBind tube, and washed twice more with cold extraction buffer. After the final wash, beads were separated on a magnetic rack to remove residual buffer and stored at -80°C for further use.   Frozen streptavidin beads were thawed and washed once with PBS prepared in HPLC-grade water (Thermo Fisher, catalog #022934-k7). The beads were transferred to a new 1.5 mL LoBind tube and washed five additional times with PBS in HPLC-grade water. After the final wash, beads were separated on a magnetic rack, and the buffer was carefully removed. Beads were then incubated with 80 µL trypsin digestion buffer containing 50 mM Tris (pH 7.5), 1 M Urea, 4 mM DTT, and 0.4 µg Trypsin at 25°C for 3 h with shaking at 1,200 rpm. Following incubation, beads were magnetically separated and washed twice with 60 µL of 1 M urea in 50 mM Tris (pH 7.5). The resulting supernatants were pooled and treated with 10 mM iodoacetamide at 25°C for 45 min in the dark with shaking at 1,200 rpm to alkylate cysteines. Digestion was continued by adding 0.5 µg of additional trypsin, followed by overnight incubation at 25°C with shaking at 1,200 rpm. The next day, a final 0.5 µg of trypsin was added, and samples were incubated for an additional 4 h at 25°C with shaking. Following digestion, 1% formic acid was added to acidify the samples, which were then vortexed and desalted using OMIX C18 pipette tips (10-100 µL, Agilent, catalog #A57003100) according to the manufacturer's instructions. Peptides were dried using a speed vacuum centrifuge and resuspended in 0.1% formic acid for LC-MS/MS analysis. Samples were analyzed using a Q-Exactive HF hybrid quadrupole-Orbitrap mass spectrometer (Thermo Fisher), coupled to an Easy-nLC 1200 ultra-performance liquid chromatography system (Thermo Fisher)."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Mass spectrometry data were analyzed using MaxQuant (version 2.4.2.0) and Perseus (version 2.0.10.0). For plasma membrane proteome comparisons between wild type and cesa3je5, raw data from TbID-YFP-LTI6b/Col-0, Col-0, TbID-YFP-LTI6b/cesa3je5, and cesa3je5 were searched together in MaxQuant using default parameters with the following modifications. The LFQ minimum ratio count was set to 2. Peptides were searched against the TAIR10 protein database (“TAIR10_pep_20101214”;  https://www.arabidopsis.org/download/list?dir=Proteins%2FTAIR10_protein_lists), supplemented with a custom list of potential contaminants, such as trypsin, human keratin, streptavidin, BSA, YFP, TbID-YFP, along with the standard MaxQuant contaminant list. “Match between runs” was enabled with a match time window of 0.4 min and an alignment time window of 20 min. The resulting “proteinGroups.txt” file was imported into Perseus with LFQ intensities as the Main category. Proteins marked with reverse, contaminant, and only identified by site identifications were removed. Data were log2-transformed, grouped, and filtered to retain proteins with at least two valid values in at least one group. Data were imputed by replacing missing LFQ values from normal distribution using the total matrix mode with a width of 0.3 and down shift of 1.8. To remove all unspecific background labeling, each TbID-YFP-LTI6b-tagged group was compared to its respective genetic background by a one-sided Welch’s t-test with S0 of 0.5, FDR of 0.05, and 250 randomizations. The resulting filtered matrix was then used to compare TbID-YFP-LTI6b/cesa3je5 and TbID-YFP-LTI6b/Col-0 using a two-sided Student’s t-test with S0 of 0.5, FDR of 0.05, and 250 randomizations."],"omics_type":["Proteomics"],"labhead":["Shouling Xu"],"instrument_platform":[""],"labhead_affiliation":["Carnegie Mass Spectrometry Facility"],"submission_type":["PARTIAL"],"species":["Arabidopsis Thaliana (mouse-ear Cress)"],"publication":["10.1016/J.CELL.2026.05.009"],"submitter_mail":["sxu@ciw.edu"],"submitter_affiliation":["Carnegie Institution at Stanford"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Identification of plasma membrane protein signatures in the cellulose-deficient mutant cesa3je5","description":"The outer cell surface of an organism is the frontline for detecting and responding to environmental stimuli. In plants, this interface consists of the plasma membrane that lies beneath the cell wall and remains associated with it through attachment sites. These wall-membrane attachments become evident upon hyperosmotic shock, when severe water loss causes the membrane to retract from the wall. Despite their long-standing observation, the molecular identity and function of these attachments remain poorly understood. Here, we identified a Cellulose Synthase Complex (CSC) nanodomain-mediated mechanism governing wall-membrane attachments: CSC density at the plasma membrane positively correlates with resistance to hyperosmotic stress. To identify membrane protein signatures in the cellulose-deficient mutant cesa3je5, we used a biotin ligase-based proximity labeling approach by expressing a TurboID (TbID)-YFP-LTI6b fusion protein in the wild type and the cesa3je5 genetic 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