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Christina Stolze"],"technology_type":["Affinity purification coupled with mass spectrometry proteomics","Mass Spectrometry","Bottom-up proteomics","Data-independent acquisition"],"software":[""],"submitter_keywords":["Inositol pyrophosphates","Phosphate homeostasis","Plants"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD073760"],"tissue":["Plant Cell"],"sample_protocol":["Root and shoot material of Arabidopsis was prepared as previously described.[14] Tissue was ground in liquid nitrogen and extracted with magnesium-containing lysis buffer. DTT was included for Affi-Gel and custom linker (20) experiments but omitted for commercial linker (21) to prevent disulfide reduction. Lysates were clarified by centrifugation and directly used for enrichment. To probe non-covalent interactions, amino-functionalized PCP analogs of 4/6-PP-InsP5 (4/5) were immobilized on NHS-activated agarose beads, according to Furkert et al. Negative control matrices contained immobilized inorganic phosphate coupled to the same linker. Beads were incubated with clarified lysates to allow equilibrium binding, then extensively washed. Bound proteins were eluted with 20 mM InsP6 (6) (elution fraction), while remaining proteins were subjected to on-bead trypsin digestion (on-bead fraction). Both fractions were analyzed by LC-MS/MS. The workflow was adapted from Wu et al. and Schneider et al. In parallel, a photoaffinity-based approach was used to covalently capture protein interactions, adapted from Haas et al.[33] Two biotinylated capture compounds were applied, both comprising a non-hydrolyzable analog of 4/6‑PP‑InsP5 (4/5), a photoreactive group, and a sorting handle. Prior to probe addition, lysates were either left untreated or pre-incubated with a 300-fold excess of soluble competitors - enantiopure 4-PP-InsP5 (4) or 6-PP-InsP5 (5). Capture compounds were added and incubated at 4 °C, followed by UV irradiation (365 nm, 30 min) to induce covalent crosslinking. Resulting complexes were isolated using streptavidin magnetic beads. After washing, beads were stored at -80 °C.   Sample preparation (on-bead digest for Affigel and Streptavidin pulldowns) Enriched proteins were submitted to an on-bead digestion using trypsin. In brief, dry beads were re-dissolved in 25 µL digestion buffer 1 (50 mM Tris, pH 7.5, 2M urea, 1mM DTT, 5 ng/µL trypsin) and incubated for 30 min at 30 °C in a Thermomixer with 400 rpm. Next, beads were pelleted and the supernatant was transferred to a fresh tube. Digestion buffer 2 (50 mM Tris, pH 7.5, 2M urea, 5 mM CAA) was added to the beads, after mixing the beads were pelleted, the supernatant was collected and combined with the previous one. The combined supernatants were then incubated o/n at 32 °C in a Thermomixer with 400 rpm; samples were protected from light during incubation. The digestion was stopped by adding 5 µL 20% TFA and desalted with C18 Empore disk membranes according to the StageTip protocol (Rappsilber et al, Anal. Chem. 2003, 75, 663.) and dried in a vacuum evaporator.   Sample preparation (in-solution digest for Affigel elutions). The eluted protein mixtures were reduced with dithiothreitol, alkylated with chloroacetamide, and digested with trypsin (0.125 µg). These digested samples were desalted using with C18 Empore disk membranes according to the StageTip protocol (Rappsilber et al, Anal. Chem. 2003, 75, 663) and dried in a vacuum evaporator. Dried peptides were re-dissolved in 2% ACN, 0.1% TFA (10 µL) for analysis. Streptavidin pulldown samples were analyzed using an EASY-nLC 1200 (Thermo Fisher) coupled to a Q Exactive Plus mass spectrometer (Thermo Fisher). Peptides were separated on 16 cm frit-less silica emitters (MSWil, 75 µm inner diameter), packed in-house with reversed-phase ReproSil-Pur C18 AQ 1.9 µm resin (Dr. Maisch). Peptides were loaded on the column and eluted for 115 min using a segmented linear gradient of 5% to 95% solvent B (0 min : 5%B; 0-5 min -> 5%B; 5-65 min -> 20%B; 65-90 min ->35%B; 90-100 min -> 55%; 100-105 min ->95%, 105-115 min ->95%) (solvent A 0% ACN, 0.1% FA; solvent B 80% ACN, 0.1%FA) at a flow rate of 300 nL/min. Mass spectra were acquired in data-dependent acquisition mode with a TOP15 method. MS spectra were acquired in the Orbitrap analyzer with a mass range of 300–1750 m/z at a resolution of 70,000 FWHM and a target value of 3×106 ions. Precursors were selected with an isolation window of 1.3 m/z. HCD fragmentation was performed at a normalized collision energy of 25. MS/MS spectra were acquired with a target value of 105 ions at a resolution of 17,500 FWHM, a maximum injection time (max.) of 55 ms and a fixed first mass of m/z 100. Peptides with a charge of +1, greater than 6, or with unassigned charge state were excluded from fragmentation for MS2, dynamic exclusion for 30s prevented repeated selection of precursors."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Affigel samples were analyzed using an Ultimate 3000 RSLC nano (Thermo Fisher) coupled to an Orbitrap Exploris 480 mass spectrometer equipped with a FAIMS Pro interface for Field asymmetric ion mobility separation (Thermo Fisher). Peptides were pre-concentrated on an Acclaim PepMap 100 pre-column (75 µM x 2 cm, C18, 3 µM, 100 Å, Thermo Fisher) using the loading pump and buffer A** (water, 0.1% TFA) with a flow of 7 µl/min for 5 min. Peptides were separated on 16 cm frit-less silica emitters (MSWil, 75 µm inner diameter), packed in-house with reversed-phase ReproSil-Pur C18 AQ 1.9 µm resin (Dr. Maisch). Peptides were loaded on the column and eluted for 130 min using a segmented linear gradient of 5% to 95% solvent B (0 min : 5%B; 0-5 min -> 5%B; 5-65 min -> 20%B; 65-90 min ->35%B; 90-100 min -> 55%; 100-105 min ->95%, 105-115 min ->95%, 115-115.1 min -> 5%, 115.1-130 min ->5%) (solvent A 0% ACN, 0.1% FA; solvent B 80% ACN, 0.1%FA) at a flow rate of 300 nL/min. Mass spectra were acquired in data-dependent acquisition mode with a TOP_S method using a cycle time of 2 seconds. For Field asymmetric ion mobility separation (FAIMS) two compensation voltages (-45 and -60) were applied, the cycle time for each experiment was set to 1 second. MS spectra were acquired in the Orbitrap analyzer with a mass range of 320–1200 m/z at a resolution of 60,000 FWHM and a normalized AGC target of 300%. Precursors were filtered using the MIPS option (MIPS mode = peptide), the intensity threshold was set to 5000, Precursors were selected with an isolation window of 1.6 m/z. HCD fragmentation was performed at a normalized collision energy of 30%. MS/MS spectra were acquired with a target value of 75% ions at a resolution of 15,000 FWHM, at an automated injection time and a fixed first mass of m/z 100. Peptides with a charge of +1, greater than 6, or with unassigned charge state were excluded from fragmentation for MS2, dynamic exclusion for 40s prevented repeated selection of precursors. Raw data were processed using MaxQuant software (version 1.6.3.4, http://www.maxquant.org/) (Cox et al., Nat. Biotechnol. 2008, 26, 1367.) with label-free quantification (LFQ) and iBAQ enabled (Cox et al., Nat. Protoc. 2016, 11, 2301.).  MS/MS spectra were searched by the Andromeda search engine against a combined database containing the sequences from A. thaliana (TAIR10_pep_20101214; ftp://ftp.arabidopsis.org/home/tair/Proteins/TAIR10_protein_lists/) and sequences of 248 common contaminant proteins and decoy sequences. Trypsin specificity was required and a maximum of two missed cleavages allowed. Minimal peptide length was set to seven amino acids. Carbamidomethylation of cysteine residues was set as fixed, oxidation of methionine and protein N-terminal acetylation as variable modifications. The match between runs option was enabled. Peptide-spectrum-matches and proteins were retained if they were below a false discovery rate of 1% in both cases.  Statistical analysis of the MaxLFQ values was carried out using Perseus (version 1.5.8.5, http://www.maxquant.org/). Quantified proteins were filtered for reverse hits and hits “identified by site” and MaxLFQ values were log2 transformed. After grouping samples by condition only those proteins were retained for the subsequent analysis that had two valid values in one of the conditions. Two-sample t-tests were performed using a permutation-based FDR of 5%. Alternatively, quantified proteins were grouped by condition and only those hits were retained that had three valid values in one of the conditions. Missing values were imputed from a normal distribution (1.8 downshift, separately for each column). Volcano plots were generated in Perseus using an FDR of 5% and an S0=1.  The Perseus output was exported and further processed using Excel."],"omics_type":["Proteomics"],"labhead":["Hirofumi Nakagami"],"instrument_platform":[""],"labhead_affiliation":["Basic Immune System of Plants / Protein Mass Spectrometry Max Planck Institute for Plant Breeding Research Carl-von-Linne-Weg 10, 50829 Cologne, Germany"],"submission_type":["PARTIAL"],"species":["Arabidopsis Thaliana (mouse-ear Cress)"],"publication":["41766624 Ritter K, Gaugler V, Stolze SC, Ghosh R, Jayamon A, Yadav R, Wollensack F, Laha D, Nakagami H, Schaaf G, Jessen HJ. Affinity-Based Interactome Mapping of Inositol Pyrophosphates Reveals 4/6-PP-InsP&lt;sub&gt;5&lt;/sub&gt;-Binding Proteins in Plants. Adv Sci (Weinh). 2026 13(26):e24290 10.1002/advs.202524290"],"submitter_mail":["stolze@mpipz.mpg.de"],"submitter_affiliation":["Plant Proteomics and Mass Spectrometry Group\nMax Planck Institute for Plant Breeding Research\nCarl-von-Linné Weg 10\n50829 Cologne"],"submitter_country":["Germany"],"pubmed_abstract":["Inositol pyrophosphates (PP-InsPs) are central regulators of eukaryotic signaling events. While certain PP-InsP isomers have been conclusively linked to the regulation of phosphate homeostasis through interaction with SPX domain-containing proteins in plants, the functions of the recently discovered isomer 4/6-PP-InsP<sub>5</sub> remain largely unknown. Here, we employ two complementary affinity-based strategies-a matrix approach and a photoaffinity probe-to systematically identify 4/6-PP-InsP<sub>5</sub>-binding proteins in Arabidopsis thaliana. The two methods yield partially overlapping protein sets, with photoaffinity enrichment likely capturing additional transient and/or weak interactions. Moreover, competition experiments with different isomers are applied to obtain information about potential isomer-specific interactions. As a proof-of-concept, one candidate interactor (FHA domain-containing protein AtFHA2) is shown to bind 4-PP-InsP<sub>5</sub> in vitro with markedly higher affinity than InsP<sub>6</sub>, while no reliable binding parameters could be obtained for its enantiomer 6-PP-InsP<sub>5</sub>. Thus, besides the SPX domain, FHA domain-containing proteins, of which 18 exist in Arabidopsis, are potentially regulated by inositol pyrophosphates. More generally, our findings reveal a diverse protein network associated with 4/6-PP-InsP<sub>5</sub> and establish a versatile platform for dissecting its biological roles in plants and other organisms."],"pubmed_title":["Affinity-Based Interactome Mapping of Inositol Pyrophosphates Reveals 4/6-PP-InsP&lt;sub&gt;5&lt;/sub&gt;-Binding Proteins in Plants."],"pubmed_authors":["Ritter Kevin K, Gaugler Verena V, Stolze Sara Christina SC, Ghosh Riya R, Jayamon Akhila A, Yadav Ranjana R, Wollensack Felix F, Laha Debabrata D, Nakagami Hirofumi H, Schaaf Gabriel G, Jessen Henning Jacob HJ"],"additional_accession":[]},"is_claimable":false,"name":"Affinity-Based Interactome Mapping of Inositol Pyrophosphates Reveals 4/6-PP-InsP5-–Binding Proteins in Plants","description":"Inositol pyrophosphates (PP-InsPs) are central regulators of eukaryotic signaling events. While certain PP-InsP isomers have been conclusively linked to the regulation of phosphate homeostasis through interaction with SPX domain containing proteins in plants, the functions of the recently discovered isomer 4/6-PP-InsP5 remain largely unknown. Here, we employed two complementary affinity-based strategies – a matrix approach and a photoaffinity probe – to systematically identify 4/6-PP-InsP5-binding proteins in Arabidopsis thaliana. The two methods yielded partially overlapping protein sets, with photoaffinity enrichment likely capturing additional transient and/or weak interactions. Moreover, competition experiments with different isomers were applied to obtain information about potential isomer-specific interactions. As a proof-of-concept, one candidate interactor (FHA domain-containing protein AtFHA2) was shown to bind 4-PP-InsP5 in vitro with markedly higher affinity than InsP6, while no reliable binding parameters could be obtained for its the enantiomeric isomer 6-PP-InsP5. Thus, besides the SPX domain, FHA domain containing proteins, of which 18 exist in Arabidopsis, are potentially regulated by inositol pyrophosphates. More generally, our findings reveal a diverse protein network associated with 4/6-PP-InsP5 and establish a versatile platform for dissecting its biological roles in plants and other organisms.","dates":{"publication":"2026-06-08","submission":"2026-01-29"},"accession":"PXD073760","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2737160","NEWT:2042546","NEWT:148942","NEWT:193528","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:89187","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:57577","NEWT:156563","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:44270","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:93217","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:10031","NEWT:82569","NEWT:661410","NEWT:488003","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:2433","NEWT:1190602","NEWT:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:1176302","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:77151","NEWT:317447","NEWT:698761","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:1177","NEWT:11308","NEWT:12637","NEWT:2164133","NEWT:1180","NEWT:2767846","NEWT:1343074","NEWT:314344","NEWT:108061","NEWT:143292","NEWT:2767842","NEWT:314345","NEWT:224308","NEWT:3134131","NEWT:49928","NEWT:160621","NEWT:110368","NCBITaxon:5204","NEWT:1916073","NEWT:1303873","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:160620","NCBITaxon:77643","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1410384","NEWT:1310173","NEWT:1072569","NEWT:1072568","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:135666","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1336794","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3710","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:65121","NEWT:3716","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:118221","NEWT:32201","NEWT:34869","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:284811","NEWT:2902907","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:34875","NEWT:10882","NEWT:1431297","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:1423687","NEWT:657322","NEWT:10886","NEWT:3707","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:1301262","NEWT:319224","NEWT:2305479","NEWT:215451","NEWT:460519","NEWT:272843","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:223074","NEWT:2499525","NEWT:467144","NEWT:142786","NEWT:28196","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:387344","NEWT:657318","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:272831","NEWT:987059","NEWT:491","NEWT:422203","NEWT:460523","NEWT:2422","NEWT:2423","NEWT:3755","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","NEWT:123606","NEWT:1195466","NEWT:2483192","NEWT:85698","NEWT:291146","NEWT:233271","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:34839","NEWT:476","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NEWT:106299","NCBITaxon:50557","NEWT:63363","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:714485","NEWT:445","NEWT:427924","NEWT:2003758","NEWT:29486","NEWT:63366","NEWT:64697","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:1120755","NEWT:1862567","NEWT:591090","NEWT:30455","NEWT:28141","NEWT:9030","NEWT:9031","NEWT:3728","NEWT:29471","NEWT:108931","NEWT:219799","NEWT:1325292","NEWT:219798","NEWT:548","NEWT:150475","NEWT:546","NEWT:1431340","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:451515","NEWT:8673","NEWT:550","NEWT:10804","NEWT:52694","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:40686","NEWT:1225786","NEWT:366497","NEWT:771870","NEWT:8665","NEWT:51338","NEWT:771875","NEWT:377142","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:311339","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:2585209","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:536","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:480020","NEWT:51315","NEWT:52641","NEWT:353152","NEWT:116597","NEWT:353153","NEWT:116598","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:6055","NEWT:13037","NEWT:518","NEWT:519","NEWT:941638","NEWT:511","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:13064","NEWT:529120","NEWT:7375","NEW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