{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079448/Sample_list.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079448/checksum.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079448/sample_description.sdrf.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079448/260522_Parashar_21579_130min_2ul.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079448/260522_Parashar_21575_130min_2ul.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079448/260522_Parashar_21581_130min_2ul.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079448/260522_Parashar_21573_130min_2ul.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079448/260522_Parashar_21578_130min_2ul.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079448/260522_Parashar_21576_130min_2ul.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079448/260522_Parashar_21580_130min_2ul.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079448/260522_Parashar_21574_130min_2ul.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079448/260522_Parashar_21577_130min_2ul.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079448/260522_Parashar_21572_130min_2ul.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079448/SwissProt_Homo_sapiens_20260507.fasta"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079448/MaxQuant_txt.zip"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["lluis.fajas@unil.ch"],"submitter":["Lluis Fajas"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"disease":["Breast Cancer"],"software":[""],"submitter_keywords":["Cdk4","Actomyosin contractility","Myo9b","Actin cytoskeleton","Cell migration","Triple negative breast cancer (tnbc)"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD079448"],"tissue":["Cell Culture"],"sample_protocol":["Tissue extracts in buffer were supplemented with concentrated reagents to reach, respectively,  4% (w/v) SDS and 20 mM DTT and heated at 75C for 10 min with agitation. After dilution 1:1 with water to reach 2% SDS, extracts were shaken with ceramic beads in in a Fastprep system for 30s to optimize extraction. Samples were cleared by centrifugation for 10 min at 10’000 x g. Supernatants were taken and their protein concentration was determined  by the tryptophane fluorescence method (Wisniewski et al., 2015, Anal Chem 87(8): 4110-4116). Proteins were digested following the SP3 protocol (Hughes et al., 2019, Nature Protocols 14(1): 68–85). Briefly, iodoacetamide was added to a final concentration of 30 mM, and cysteines in samples were alkylated for 45 min in the dark. Sera-Mag™ SpeedBeads (Cytiva, 45152105050250) were added at a 10:1 (w:w) bead-to-protein ratio, and proteins were precipitated on the beads using ethanol (final concentration 60%). After three washes with 80% ethanol, proteins were digested on-bead in 50 µL of 100 mM ammonium bicarbonate containing 1.0 ug trypsin/LysC mix (Promega, # V5073) for 1.5 h at 37 °C. The same quantity of trypsin was then added, and incubation continued for another 1.5h. Supernatants were collected and mixed with two sample volumes of isopropanol containing 1% TFA, followed by desalting on an SCX plate (Oasis MCX 96-well, 186001830BA; WatersTM) to remove residual SDS. After washing with isopropanol/1% TFA and 2% acetonitrile/0.1% FA, peptides were eluted in 150 µL of 40% MeCN, 59% water, and 1% (v/v) ammonia, then dried by centrifugal evaporation. Tryptic peptide mixtures were injected on a Vanquish Neo nanoHPLC system interfaced via a nanospray Flex source to a high resolution Orbitrap Exploris 480 mass spectrometer (Thermo Fisher, Bremen, Germany). Peptides were loaded onto a trapping microcolumn PepMap100 C18 (5 mm x 1.0 mm ID, 5 μm, Thermo Fisher) before separation on a C18 custom packed column (75 μm ID × 45 cm, 1.8 μm particles, Reprosil Pur, Dr. Maisch), using a gradient from 2 to 80 % acetonitrile in 0.1 % formic acid for peptide separation at a flow rate of 250 nl/min (total time: 130 min). Full MS survey scans were performed at 120,000 resolution. A data-dependent acquisition method controlled by Xcalibur software (Thermo Fisher Scientific) was used that optimized the number of precursors selected (“top speed”) of charge 2+ to 5+ while maintaining a fixed scan cycle of 2 s. Peptides were fragmented by higher energy collision dissociation (HCD) with a normalized energy of 30 % at 15’000 resolution. The window for precursor isolation was of 1.6 m/z units around the precursor and selected fragments were excluded for 60s from further analysis."],"repository":["pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Data files were processed using MaxQuant (version 2.6.7 ;  Cox et al., 2008, Nat Biotechnol 26: 1367–1372) integrated with the Andromeda search engine (Cox et al., 2011, J Proteome Res 10(4): 1794–1805). Carbamidomethylation of cysteine was set as a fixed modification, while methionine oxidation and protein N-terminal acetylation were specified as variable modifications. Database searches were performed again the human subset of the SWISSPROT database (www.uniprot.org; release of May 2026,  20’670entries ). Alternatively, both the human and mouse SWISSPROT databases (release of October 2025, 17’855 entries) were searched to account for the presence of proteins from both species. A contaminant database including common environmental contaminants and digestion-related enzymes (e.g., keratins, trypsin) was used in all cases (Frankenfield et al., J Proteome Res 21(9): 2104-2113). Mass tolerances were set to 4.5 ppm for precursor ions (after recalibration) and 20 ppm for MS/MS fragments. Peptide and protein identifications were filtered at a 1% false discovery rate (FDR) based on matches to a decoy database generated by reversing protein sequences. Label-free quantitation of proteins was carried out in MaxQuant using the match between runs function and the MaxLFQ algorithm (Cox et al 2014, Molecular & Cellular Proteomics 13(9): 2513–26)."],"omics_type":["Proteomics"],"labhead":["Lluis Fajas Coll"],"instrument_platform":[""],"labhead_affiliation":["Center for Integrative Genomics, CIG, UNIL Sorge, CH1015 Lausanne, Switzerland"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["10.1101/2025.08.06.668850"],"submitter_mail":["lluis.fajas@unil.ch"],"submitter_affiliation":["UNIL"],"submitter_country":["Switzerland"],"additional_accession":[]},"is_claimable":false,"name":"Cyclin Dependent Kinase 4 (CDK4) maintains cell cytoskeleton integrity and behavior in Triple Negative Breast Cancer (TNBC) cells","description":"Cyclin-Dependent Kinase 4 (CDK4) is best known for its role in cell cycle progression, but its contribution to cellular architecture is less understood. Here, we identify CDK4 as a regulator of cytoskeletal homeostasis in triple-negative breast cancer (TNBC). CDK4 phosphorylates the RhoGAP Myo9b at serine 1935, enhancing its activity and suppressing RhoA–ROCK–mediated actomyosin contractility. Loss or inhibition of CDK4 disrupts cell morphology, destabilizes the actin cytoskeleton, and increases contractility, alongside collapse of the intermediate filament network, including vimentin disorganization and altered mitochondrial distribution. CDK4-deficient cells also show faster but less directed migration. In vivo, tumors derived from CDK4WT and CDK4KO MDA-MB-231 cells implanted in the mammary fat pad display elevated pMLC levels by IHC, consistent with increased contractility, while proteomic analysis reveals enrichment of cytoskeletal pathways. Transcriptomic analyses (SCAN-B, TCGA, I-SPY2) further show that low CDK4 activity correlates with enhanced EMT, migration, metastasis, and RhoA signaling programs in TNBC. Together, these findings establish CDK4 as an upstream regulator of cytoskeletal integrity, linking actin dynamics, intermediate filament organization, and cell behavior, and reveal a structural role beyond its canonical function in cell cycle 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