{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067224/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067224/20240815_HF_LC3_GF_RK_12005_01_19.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067224/20240815_HF_LC3_GF_RK_12005_01_20.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067224/20240815_HF_LC3_GF_RK_12005_01_9.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067224/20240815_HF_LC3_GF_RK_12005_01_8.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067224/20240815_HF_LC3_GF_RK_12005_01_7.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067224/20240815_HF_LC3_GF_RK_12005_01_21.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067224/fragger.params","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067224/fragpipe-files.fp-manifest","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067224/fragpipe.workflow"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["knapp@pharmchem.uni-frankfurt.de"],"submitter":["Thorsten Mosler"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Protac","Limk"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067224"],"sample_protocol":["Purified Flag-CRBN was conjugated to Flag beads (cat no) in IP buffer (50mM Tris pH-7.5, 120mM NaCl, 1% NP40, 0.5mM EDTA) for 1hr at 40C on a rotating shaker, before addition of DMSO or 5µM NAN69 for 30min at 40C. Subsequently, 1mg of freshly prepared protein lysate from Molt4 cells was added to the prepared beads in IP lysate buffer (50mM Tris pH-7.5, 120mM NaCl, 1% NP40, 0.5mM EDTA, protease inhibitors, phosphatase inhibitors and NEM) for 1hr at 40C while rotating. The beads were washed three times with IP buffer and afterwards used either for western blotting or trypsin digestion followed by LC-MS2 analysis.  Protein-bound flag-CRBN beads were incubated with 20 µl SDC buffer (3% sodium deoxycholate in 50 mM Tris-HCl pH 8.5) and heated for 5min at 65°C and supernatant was collected. This step was repeated one more time to get elute of 40µl. Further, reduction and alkylation were performed using 5ul of 5mM TCEP, 20mM CAA in 50 mM Tris-HCl pH 8.5 at 95°C for 10min. 500 ng of trypsin in 45 µl 50 mM Tris-HCl (pH 8.5) was added to each sample and kept it for digestion at 37 °C overnight. The digestion was stopped upon addition of 150 µl of 1% TFA in isopropanol. Peptide clean-up was performed using SDB-RPS stage tips (Sigma-Aldrich). Peptides were added to stage tips and washed first with 1% TFA in isopropanol and then with 0.2% TFA in water. Lastly, peptides were eluted in 80% acetonitrile plus 1.25% ammonia and dried in vacuum concentrator. Dried peptides were resuspended in 2%ACN with 0.1% TFA and used for LC-MS2 analysis on a QExactive HF mass spectrometer coupled to an easy nLC 1200 (Thermo Fisher Scientific) fitted with a 35 cm long, 75µm ID fused-silica column packed in house with 1.9 µm C18 particles (Reprosil pur, Dr. Maisch). The column was maintained at 40 °C using an integrated column oven (Sonation). Peptides were eluted in a non-linear gradient of 5–40% acetonitrile over 60 min and sprayed into the mass spectrometer equipped with a nanoFlex ion source (Thermo Fisher Scientific). Full-scan MS spectra (300–1,650 m/z) were acquired in profile mode at a resolution of 60,000 at m/z 200, a maximum injection time of 20 ms and an AGC (automatic gain control) target value of 3 × 106. Up to 10 of the most intense peptides per full scan were isolated using a 1.4-Th window for fragmentation by higher energy collisional dissociation (normalized collision energy of 27). MS/MS spectra were acquired in centroid mode with a resolution of 30,000, a maximum injection time of 54 ms and an AGC target value of 1 × 105. Single charged ions, ions with a charge state of more than seven and ions with unassigned charge states were not considered for fragmentation, and dynamic exclusion was set to 20 s to minimize the acquisition of fragment spectra representing already acquired precursors."],"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":[""],"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"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["thorstenmosler@googlemail.com"],"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_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 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