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Cells were collected and nuclear protein extract is collected using Nuclear Extract Kit (Active Motif, 40010). A total of 600 µg of nuclear protein lysate was incubated with 60 µL of magnetic streptavidin beads, which had been pre-washed twice with RIPA lysis buffer. The mixture was brought to a final volume of 1 mL by adding additional RIPA buffer and incubated overnight at 4 °C on a rotator. Following incubation, streptavidin beads were collected using a magnetic rack, and the supernatant was transferred to new tubes. The beads were subsequently washed twice with 1 mL of RIPA lysis buffer, once with 1 mL of 1.0 M KCl, once with 1 mL of 50 mM TEAB buffer, and twice with Tris-HCl (pH 7.5). Sample preparation was conducted as described previously with minor modifications. [PMID: 40022872, PMID: 40345165] The bead-bound proteins were reconstituted in 75 µL of 100 mM triethylammonium bicarbonate (TEAB) to adjust the pH to 8.0. Proteins were then reduced by adding 5 µL of 50 mM dithiothreitol (DTT) and incubated at 60 °C for 1 hour on a shaker. Samples were subsequently cooled and alkylated with 5 µL of 100 mM iodoacetamide (IAA) for 15 minutes in the dark on a shaker. Alkylation was quenched by adding 5 µL of 50 mM DTT. Protein digestion was performed using a mixture of Lys-C and trypsin and incubated at 37 °C overnight on a shaker at 1,100 rpm. The enzyme amounts were determined based on the estimated amount of target protein calculated from the bead binding capacity, resulting in an approximate enzyme-to-protein ratio of 1:40. Subsequently, the samples were desalted on using an HLB u-elution solid-phase extraction plate (Waters). The eluted peptide solution was subsequently dried under vacuum using a Savant SPD121P SpeedVac concentrator (Thermo Scientific) and stored at -80 °C until further use. For quantitative mass spectrometry, 9-plex tandem mass tag (TMT) pro reagents (Thermo Fisher Scientific) were used to label digested peptide samples according to the manufacturer’s instructions. Peptides were resuspended in 50 µL of 100 mM triethylammonium bicarbonate (TEAB), and the TMT reagent was dissolved separately in 20 µL of anhydrous acetonitrile. The peptide solution was then mixed with 10 ul of the TMT reagent solution which is half the amount needed to label 100ug.  The reaction was allowed to proceed for 1 hour and then quenched with 2.5 ul of 5% hydroxyl amine for 15 minutes. The TMT-labeled peptides were pooled and subjected to pre-fractionation using basic pH reversed-phase liquid chromatography (bRPLC) employing an Agilent 1200 offline High-Performance Liquid Chromatography (HPLC) system (Agilent Technologies, Santa Clara, CA, USA). This process entailed reconstituting peptides in solvent A (10 mM TEAB in water, pH 8.5), loading them onto a Waters XBridge column (5um, 2.1 mm x 100 mm, Waters) and resolving them over 90 minutes using a gradient of solvent B (10 mM TEAB in 90% ACN and 10% water, pH 8.5) at a flow rate of 250 ul/min. This resulted in the collection of 96 fractions, which were subsequently concatenated into 24 fractions and dried using a SpeedVac."],"repository":["Pride"],"labhead":["Danfeng Cai"],"instrument_platform":[""],"submission_type":["COMPLETE"],"labhead_affiliation":["Assistant professor, Biochemistry and Molecular Biology, Johns Hopkin Bloomberg Schools of Public Health, USA."],"publication":["10.1101/2025.05.02.651992"],"submitter_affiliation":["Johns Hopkins Bloomberg School of Public Health"],"labhead_mail":["danfeng.cai@jhu.edu"],"technology_type":["Affinity purification coupled with mass spectrometry proteomics","Mass Spectrometry"],"disease":["Papillary Renal Cell Carcinoma"],"submitter_keywords":["Human","Tead1","Ap-ms","Condensate","Kidney","Cancer"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD072858"],"quantification_method":[""],"modification":[""],"data_protocol":["The TMT labeled peptides were analyzed by reverse-phase chromatography tandem mass spectrometry on a Vanquish NEO UPLC interfaced with an Orbitrap Exploris 480 mass spectrometer (Thermo Fisher Scientific).  Peptides were separated using a 2%–90% acetonitrile in 0.1% formic acid gradient over 120 min at 300 nl/min using an in-house packed 75-um ID x 15 cm column packed with ReproSIL-Pur-120-C18-AQ (2.4 µm, 120 Å bulk phase, Dr. Maisch). Survey scans of precursor ions were acquired from 375-1500 m/z at a resolution setting of 120,000.  Precursor ions were isolated in data dependent mode with a 3 second cycle time using a 0.7 dalton isolation width and a 60s dynamic exclusion.  Peptides were fragmented at a normalized HCD collision energy of 36 with a resolution setting of 30,000 using TurboTMTPro setting and a defined first mass of 120.  Data analysis: Data analysis was conducted as described previously with minor modifications [PMID: 41216884]. The LC–MS/MS–derived MS/MS spectra were searched against the UniProt human protein database (UP5640_H_sapiens_20240916), including both reviewed (Swiss-Prot) and unreviewed (TrEMBL) entries, supplemented with common contaminant proteins and reversed decoy sequences for false discovery rate (FDR) estimation. Database searching was carried out using the CHIMERYS algorithm (Inferys 4.7.0 prediction model) implemented in Proteome Discoverer (version 3.2.0.450, Thermo Scientific). Trypsin was specified as the proteolytic enzyme, allowing up to two missed cleavages. Carbamidomethylation of cysteine residues (+57.02146 Da) and TMTpro labeling (+304.20715 Da) on lysine residues and peptide N-termini were set as fixed modifications, while oxidation of methionine (+15.99492 Da) was included as a variable modification. Peptide length was constrained to 7–30 amino acids, and the fragment ion (MS2) mass tolerance was set to 20 ppm. An FDR threshold of 1% was applied at the PSM, peptide, and protein levels using the CHIMERYS internal percolator strategy. For protein quantification, MS2-based reporter ion quantification was performed using HCD fragmentation. Reporter ions were integrated using the most confident centroid with a mass tolerance of 20 ppm, and reporter ion intensities were calculated based on signal-to-noise ratios. Reporter ion abundances were calculated from signal-to-noise ratios, with a minimum average S/N threshold of 10 and a co-isolation interference threshold of 65% and a Normalized CHIMERYS Coefficient of 0.45. Protein quantification was based on both unique and razor peptides under the strict parsimony principle, and protein groups lacking unique peptides were excluded. Final protein groups were generated by iteratively evaluating all spectra, selecting peptide-spectrum matches (PSMs) assigned to the protein group with the highest number of unambiguous peptides, and summing the corresponding reporter ion abundances across those PSMs.  Statistical analysis and bioinformatics  Experimental design and statistical analyses were performed as described previously with minor modifications [PMID: 40596376]. Statistical analysis of the mass spectrometry data was carried out using the Perseus software package (version 1.6.15.0) (PMID: 27348712). Proteins with a q-value < 0.05 were considered significantly differentially expressed between the compared groups. To ensure proper normalization, the intensity values of each protein underwent two normalization steps: first, protein abundance values across the samples were divided by the median abundance value of each protein, followed by dividing protein abundance values across the proteins by the median abundance value of each sample. The relative abundance values of each sample were then log2-transformed. According to our normality test using the Shapiro–Wilk test in the dplyr package in R, the protein abundances showed normal distribution. Thus, P values were computed using Student's two-sample t-test for intergroup comparisons. To address multiple comparisons, the FDR was calculated by comparing data with and without permutations between groups. The q-values were determined using a permutation-based FDR estimation method within the Significance Analysis of Microarrays (SAM) approach [PMID: 11309499]. Proteins exhibiting significant differences in protein abundance were subjected to Gene Ontology (GO) analysis using the Enrichr [PMID: 27141961]."],"omics_type":["Proteomics"],"species":["Homo Sapiens (human)"],"submitter_mail":["danfeng.cai@jhu.edu"],"submitter_country":["United States"],"doi":["10.6019/PXD072858"],"additional_accession":[]},"is_claimable":false,"name":"TEAD1 condensates are transcriptionally inactive storage sites on the pericentromeric heterochromatin","description":"TEA domain transcription factor 1 (TEAD1), a Hippo pathway transcription factor important in cellular homeostasis and development, is increasingly implicated in cancer biology. Here, we reveal a novel role for TEAD1 in organizing nuclear condensates, independent of active transcription. Using high-resolution imaging, ChIP-seq, RNA-seq and proximity-based proteomics, we demonstrate that in patient-derived renal cell carcinoma cells, TEAD1 forms micron-sized foci by binding to the heterochromatic pericentromeric regions using its DNA-binding domain. These TEAD1 foci do not mediate transcription but instead serve as depots for excess TEAD 1. This contrasts with TEAD1 organization in other genomic regions of both RCC and normal kidney cells, where TEAD1 associates with markers of active transcription. Our findings provide a mechanistic framework for TEAD1’s dual regulatory roles, offering new insights into its contribution to transcriptional dysregulation and tumor progression.","dates":{"publication":"2026-04-27","submission":"2026-01-09"},"accession":"PXD072858","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:661410","NEWT:638632","NEWT:224326","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: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:7719","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: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: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:177437","NEWT:717966","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","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:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:485","NEWT:56636","NEWT:2499525","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: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: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:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","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:9541","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:10804","NEWT:33941","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:575412","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","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