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Proteins were precipitated using methanol-chloroform and resuspended in 8 M urea, 50 mM Tris pH 8.5. Proteins were digested with 1:50 w/w LysC (Wako Chemicals, cleaves at the carboxylic side of lysine residue) and 1:100 w/w trypsin (Promega, Sequencing-grade) overnight at 37 °C after dilution to a final urea concentration of 1 M using 50 mM Tris pH 8.5. Digested peptides were then acidified (pH 2–3) using trifluoroacetic acid (TFA) and purified using C18 SepPak columns (Waters). Desalted peptides were dried and resuspended in TMT-labeling buffer (200 mM EPPS pH 8.2, 20% acetonitrile). 10μg of peptides per condition were subjected to TMT labeling with 1:2.5 peptide TMT ratio (w/w) for 1 h at room temperature. The labeling reaction was quenched by addition of hydroxylamine to a final concentration of 0.5% and incubation at room temperature for 15 min. Successful TMT labeling was verified by mixing equimolar ratios of peptides and subjecting the mix to single shot LC-MS/MS analysis. For high pH reversed phase fractionation on a Dionex analytical HPLC, 50µg of pooled and purified TMT labelled samples were resuspended in 10mM ammonium-bicarbonate (ABC), 5%ACN, and separated on a 250mm long C18 column (Aeris Peptide XB-C18, 4.6mm ID, 2.6 µm particle size; Phenomenex) using a multistep gradient from 100% Solvent A (5% ACN, 10mM ABC in water) to 60% Solvent B (90% ACN, 10mM ABC in water) over 70 minutes. Eluting peptides were collected every 45 seconds into a total of 96 fractions, which were cross-concatenated into 24 fractions and dried in a vacuum concentrator and resuspended in 3% ACN, 0.1% TFA for LC-MS analysis.Tryptic peptides were analyzed on an Orbitrap Lumos coupled to an easy nLC 1200 (ThermoFisher Scientific) using a 35 cm long, 75µm ID fused-silica column packed in house with 1.9 µm C18 particles (Reprosil pur, Dr. Maisch), and kept at 50°C using an integrated column oven (Sonation). HPLC solvents consisted of 0.1% Formic acid in water (Buffer A) and 0.1% Formic acid, 80% acetonitrile in water (Buffer B). Assuming equal amounts in each fraction, 400 ng of peptides were eluted by a non-linear gradient from 7 to 40% B over 90 minutes, followed by a step-wise increase to 90%B in 6 minutes which was held for another 9 minutes. A synchronous precursor selection (SPS) multi-notch MS3 method was used to minimize ratio compression as previously described (McAlister et al., 2014). Full-scan MS spectra (350–1400 m/z) were acquired at a resolution of 120,000 at m/z 200, a maximum injection time of 100 ms, and an AGC target value of 4*105. The most intense precursors with charge state between 2 and 6 were selected for fragmentation (“Top Speed” with a cycle time of 1.5 seconds) and isolated with a quadrupole isolation window of 0.7 Th. MS2 scans were performed in the Ion trap (Turbo) using a maximum injection time of 50 ms, AGC target value of 15000 and fragmented using CID with a normalized collision energy (NCE) of 35%. MS3 acquisition was performed on the 10 most intense MS2 fragment ions with an isolation window of 0.7 Th (MS) and 2 m/z (MS2). Ions were fragmented using HCD with an NCE of 50% and analyzed in the Orbitrap with a resolution of 50,000 at m/z 200, scan range of 100-500 m/z, AGC target value of 150000 and a maximum injection time of 86ms. All spectra were acquired in centroid mode."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["MS raw data were analyzed using FragPipe v21.1, with MSFragger v.4.0 (PMID: 28394336) and Philosopher v.5.1.0 (PMID: 32669682). The built-in workflow “LFQ-MBR” was used with a precursor mass tolerance of 20 ppm and fragment mass tolerance of 20 ppm. The human proteome database used by FP (ID: UP000005640, 20/08/2024) comprised of 20,468 reviewed sequences only and their corresponding decoys, including common contaminant proteins. Identifications were filtered to obtain false discovery rates (FDR) below 1% for both peptide spectrum matches (minimum peptide length of 7) and proteins using a target-decoy strategy. For all searches, carbamidomethylated cysteine was set as a fixed modification and oxidation of methionine and N-terminal protein acetylation as variable modifications with allowing up to 3 modifications per peptide. Strict trypsin cleavage was set as protein digestion rule. Label-free quantification was performed using IonQuant v.1.10.27 (PMID: 33813065). Data were further processed using FragPipe Analyst (PMID: 38496650. Subsequently, the data were plotted in R using custom scripts."],"omics_type":["Proteomics"],"labhead":["Stefan Knapp"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Institute of Pharmaceutical Chemistry, Goethe University, Max-von-Laue-Str. 9, 60438 Frankfurt am Main, Germany Structural Genomics Consortium (SGC), Buchmann Institute for Life Sciences, Max-von-Laue-Str. 15, 60438 Frankfurt am Main, Germany German Cancer Consortium (DKTK) Mainz/Frankfurt, German Cancer Research Center (DKFZ), 69120 Heidelberg, Germany"],"species":["Homo Sapiens (human)"],"publication":["42066056 Azeez KRA, Saraswati H, Mosler T, Hanke T, Ho-Xuan H, Neder N, Sivashanmugam SA, Heinz M, Schwalm MP, Giuliani G, Rathore R, Kazi R, Kumar R, Mitrovic M, Prieto-Garcia C, Bailey HJ, Mathea S, Hummer G, Đikić I, Müller S, Stolz A, Krause DS, Knapp S. Discovery and Development of a Potent LIMK2 Isoform-Specific Degrader. ACS Chem Biol. 2026 21(5):1158-1176 10.1021/acschembio.6c00137"],"submitter_mail":["thorstenmosler@googlemail.com"],"submitter_affiliation":["Goethe University Clinics Frankfurt"],"submitter_country":["Germany"],"pubmed_abstract":["The LIM kinases (LIMK1/2) are key mediators in signaling cascades that regulate actin cytoskeleton dynamics via cofilin phosphorylation. Dysregulation of these pathways and overexpression of LIMKs are implicated in disease development, including cancer, Fragile X syndrome, and glaucoma. Positioned downstream of actin-regulating Rho GTPase signaling pathways, LIM kinases are attractive drug targets. Here, we targeted LIMKs with PROTACs to disrupt both catalytically and noncatalytically mediated functions. Despite employing a dual LIMK1/2 inhibitor warhead and high structural conservation between the two human LIM kinases, we discovered isoform-specific LIMK2 degradation by initial PROTACs that we optimized into a highly potent and selective LIMK2 degrader. Cell-based assays and structural analysis indicated that isoform specificity was likely driven by favorable orientation bias and/or lysine accessibility, along with enhanced ternary complex formation. We comprehensively characterized the PROTAC as a chemical probe that induces isoform-specific degradation, offering a powerful alternative to conventional reversible pan-LIMK inhibitors."],"pubmed_title":["Discovery and Development of a Potent LIMK2 Isoform-Specific Degrader."],"pubmed_authors":["Azeez Kamal Rayees Abdul KRA, Saraswati Hayuningbudi H, Mosler Thorsten T, Hanke Thomas T, Ho-Xuan Hung H, Neder Noah N, Sivashanmugam Saran Aswathaman SA, Heinz Marcel M, Schwalm Martin-Peter MP, Giuliani Giulio G, Rathore Rajeshwari R, Kazi Rubina R, Kumar Rahul R, Mitrovic Marko M, Prieto-Garcia Cristian C, Bailey Henry J HJ, Mathea Sebastian S, Hummer Gerhard G, Đikić Ivan I, Müller Susanne S, Stolz Alexandra A, Krause Daniela S DS, Knapp Stefan S"],"additional_accession":[]},"is_claimable":false,"name":"Discovery and development of a potent LIMK2 isoform-specific degrader","description":"The LIM kinases (LIMK1/2) are key mediators in the multi-step signaling cascades that regulate actin cytoskeleton dynamics via cofilin phosphorylation. Dysregulation of these pathways and overexpression of LIMKs are implicated in disease development, including cancer, Fragile X syndrome, and glaucoma. Positioned downstream of the Rac/CDC42 signaling pathways, LIM kinases are attractive drug targets. Here, we targeted the LIMKs with PROTACs to disrupt both catalytic and non-catalytic mediated functions. Despite employing a dual LIMK1/2 inhibitor warhead and high structural conservation between the two human LIM kinases, we discovered isoform-specific LIMK2 degradation. We developed initial PROTACs into a highly potent and selective LIMK2 degrader. Cell-based assays and structural comparisons suggested that isoform specificity was likely driven by favorable orientation bias and/or lysine accessibility, along with enhanced ternary complex formation. Finally, we comprehensively characterized the PROTAC as a chemical probe, which induces isoform-specific degradation, which can be challenging to achieve with conventional reversible inhibitors.","dates":{"publication":"2026-05-25","submission":"2025-08-12"},"accession":"PXD067272","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:1584","NEWT:36630","NEWT:383379","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:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","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:270643","NEWT:2065263","NEWT:177437","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: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:9483","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:237610","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:108458","NEWT:5936","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:1255228","NEWT:410289","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:906914","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:49012","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:5147","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:1613","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:40674","NEWT:1194669","NEWT:443906","NEWT:13037","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:105487","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:475932","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:28550","NEWT:80863","NEWT:90675","NEWT:52639","NEWT:52638","NEWT:57075","NEWT:1666905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