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Per genotype and treatment, the rosettes of 12 plants were harvested and ground in liquid nitrogen. All plant material was used for further protein extraction. Proteins were extracted with 1 ml extraction buffer (50 mM TRIS-HCl pH 7,5, 100 mM NaCl, 10 % glycerol, 2mM EDTA, 2mM DTT, 1 % protease inhibitor cocktail, 1 % PMSF, 1% IGEPAL) per 1 ml plant material. For immunoprecipitation, GFP-Trap agarose beads (ChromoTek) were used and incubated with the crude extract for 3 h at 4 °C. Beads were washed 3 times with wash buffer (50 mM Tris-HCl pH 7.5, 50 mM NaCl, 1 mM phenylmethanesulfonyl fluoride, 0.1 % IPEGAL). Subsequently, washed beads were incubated in 50 µl of Laemmli sample buffer for 10 min at 95 °C. Next, in‐gel trypsin digestion was performed according to standard procedures (Shevchenko et al., 2006). Briefly, samples were run on a Nu-PAGE™ 4%–12% Bis‐Tris protein gel (ThermoFisher Scientific) for about 1 cm. Subsequently, the still not size‐separated single protein band per sample was cut out, reduced (50mM dithiothreitol), alkylated (55mm chloroacetamide) and digested overnight with trypsin (Trypsin Gold, mass spectrometry grade, Promega). The peptides obtained were dried to completeness and resuspended in 24 μL of 2% acetonitrile, 0.1% formic acid in HPLC grade water. Finally, 5 μL of sample were injected per mass spectrometric (MS) measurement. LC-MS/MS data acquisition was carried out on a Dionex Ultimate 3000 RSLCnano system coupled to a Q-Exactive HF-X mass spectrometer (ThermoFisher Scientific, Bremen). Peptides were delivered to a trap column (ReproSil-pur C18-AQ, 5 μm, Dr. Maisch, 20 mm × 75 μm, self-packed) at a flow rate of 5 μL/min in 0.1% formic acid in HPLC grade water. After 10 minutes of loading, peptides were transferred to an analytical column (ReproSil Gold C18-AQ, 3 μm, Dr. Maisch, 450 mm × 75 μm, self-packed) and separated using a 50 min gradient from 4% to 32% of solvent B (0.1% FA, 5% DMSO in acetonitrile) in solvent A (0.1% FA, 5% DMSO in HPLC grade water) at 300 nL/min flow rate. The Q-Exactive HF-X mass spectrometer was operated in data dependent acquisition (DDA) and positive ionization mode. MS1 spectra (360–1300 m/z) were recorded at a resolution of 60k using an automatic gain control (AGC) target value of 3e6 and maximum injection time (maxIT) of 45 msec. Up to 18 peptide precursors were selected for fragmentation. Only precursors with charge state 2 to 6 were selected and dynamic exclusion of 30 sec was enabled. Peptide fragmentation was performed using higher energy collision induced dissociation (HCD) and a normalized collision energy (NCE) of 26%. The precursor isolation window width was set to 1.3 m/z. MS2 Resolution was 15.000 with an automatic gain control (AGC) target value of 1e5 and maximum injection time (maxIT) of 25 msec."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["Protein and phosphopeptide identification and quantification were performed using the software MaxQuant (version 1.6.3.4) with its built‐in search engine Andromeda. MS2 spectra were searched against the TAIR Arabidopsis thaliana protein database (downloaded  March 2022,  48231 protein entries) supplemented with the GFP protein sequence as well as with common contaminants (built‐in option in MaxQuant). Trypsin/P was specified as proteolytic enzyme. Carbamidomethylated cysteine was set as fixed modification. Phosphorylation of serine/threonine/tyrosine, oxidation of methionine and acetylation at the protein N‐terminus were specified as variable modifications. Results were adjusted to a 1% false discovery rate on peptide spectrum match (PSM) level and protein level employing a target‐decoy approach using reversed protein sequences. The minimal peptide length was defined as 7 amino acids and the “match-between-run” functionality was enabled (matching time window 0.7 min, alignment time window 20 min). For protein quantification the MaxQuant output table proteinGroups.txt and Label-Free Quantification (LFQ) intensities were used. Only proteins detected in at least two biological replicates in at least one experimental condition were further processed. Missing values were imputed by a protein-specific constant value, which was defined as the lowest detected protein-specific LFQ-value over all samples divided by two, using the data visualisation platform omicsViewer (DOI: 10.1101/2022.03.10.483845). Additionally, a maximal imputed LFQ value was defined as 15% quantile of the protein distribution from the dataset. For phosphopeptide detection the MaxQuant output table Phospho(STY)Sites.txt was used. Only phosphosites detected on FERONIA in at least two biological replicates in at least one experimental condition were considered. The FER-GFP infected with powdery mildew and untreated experiments were performed in biological triplicates, while all other experiments were performed in biological quadruplets."],"omics_type":["Proteomics"],"labhead":["Christina Ludwig"],"instrument_platform":[""],"labhead_affiliation":["Bavarian Center for Biomolecular Mass Spectrometry (BayBioMS) School of Life Science Technical University Munich (TUM) Gregor-Mendel-Straße 4 85354 Freising GERMANY"],"submission_type":["PARTIAL"],"species":["Arabidopsis Thaliana (mouse-ear Cress)"],"submitter_mail":["tina.ludwig@tum.de"],"publication":["Not available"],"submitter_affiliation":["TU Munich"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Endogenous RALF peptide function is required for powdery mildew host colonization","description":"The receptor kinase FERONIA (FER) is a susceptibility factor for biotrophic powdery mildew fungal pathogens in Arabidopsis thaliana, but the underlying molecular mechanisms remain largely unknown. FER is required for the perception of endogenous RAPID ALKALINIZATION FACTOR (RALF) peptides to control various aspects of plant growth, development and immunity. RALFs are either perceived by FER/LORELEI-LIKE GPI-ANCHORED PROTEIN (LLG) heterocomplexes to induce cellular responses or bind to LEUCINE-RICH REPEAT EXTENSIN (LRX) proteins as cell wall structural components. Combining genetics, cell biology and biochemistry, we found that FER`s endogenous RALF ligands are necessary for full colonization success of the powdery mildew species Erysiphe cruciferarum. We reveal that LLGs and LRXs are also powdery mildew susceptibility factors. We show that cell wall remodeling and apoplastic pH homeostasis, hallmark features of RALF function, support powdery mildew reproductive success. We provide data that RALF-dependent powdery mildew pathogenesis is partially independent of FER. Powdery mildew fungi likely do not produce RALF peptide mimics, suggesting their reliance on endogenous RALFs for successful host colonization. We propose that powdery mildew fungi require RALF-mediated modulation of apoplastic pH and pectin re-modelling for successful host colonization, highlighting a new susceptibility mechanism by obligate biotrophic fungi.","dates":{"publication":"2026-05-15","submission":"2025-01-13"},"accession":"PXD059737","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:1599","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:2736291","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:294671","NEWT:376619","NEWT:1748418","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:2086595","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:381198","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:3357","NEWT:7719","NEWT:29073","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:2020713","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:2502409","NEWT:212790","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:370038","NEWT:498211","NEWT:345076","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:200795","NEWT:342808","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:329854","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:2649329","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:3715","NEWT:2065263","NEWT:199225","NEWT:177437","NEWT:717966","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:10886","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:1955249","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:2714896","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:1608994","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:1122981","NEWT:2853422","NEWT:1122984","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:119562","NEWT:1883446","NEWT:31345","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:1922344","NEWT:108458","NEWT:5936","NEWT:85692","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:279010","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:415978","NEWT:235455","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:9054","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:717989","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:1871049","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:548","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:2126348","NEWT:5180","NEWT:256737","NEWT:299467","NEWT:9541","NEWT:51350","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:542","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:2587410","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:2126337","NEWT:550","NEWT:253237","NEWT:10804","NEWT:33941",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