{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064756/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064756/20181009_JH_04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064756/20181009_JH_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064756/20181009_JH_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064756/20180413_MP_16.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064756/20180413_MP_15.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064756/20181009_JH_02.raw"],"Mgf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064756/a8a6e5221f272a39___20181009_JH_01.raw.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064756/a8a6e5221f272a39___20181009_JH_04.raw.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064756/8986d8e95f1622ea___20180413_MP_16.raw.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064756/8986d8e95f1622ea___20180413_MP_15.raw.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064756/a8a6e5221f272a39___20181009_JH_02.raw.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064756/a8a6e5221f272a39___20181009_JH_03.raw.mgf"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064756/20181009_JH_03.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064756/20181009_JH_02.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064756/20181009_JH_04.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064756/20180403_MP_15.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064756/20180403_MP_16.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064756/20181009_JH_01.dat"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["Andreja.Ambriovic.Ristov@irb.hr"],"submitter":["Nikolina Stojanovic"],"technology_type":["Mass Spectrometry","Chemical cross-linking coupled with mass spectrometry proteomics"],"disease":["Melanoma"],"software":["Not available"],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD064756"],"tissue":["Melanocyte","Cell Culture"],"sample_protocol":["Samples (prepared in triplicates) were processed as previously described (Jones et al., 2015, Paradzik et al., 2020). In short, cells (2-2.5x106, depending on what the cells were transfected with, to obtain similar cell number 48 hours later) were plated on 10 cm diameter cell culture dishes (at least 6 dishes per cell line) and grown in DMEM supplemented with 10% (v/v) FBS. After 48 hours, the medium was removed, cells were washed with DMEM-HEPES (hydroxyethyl piperazineethanesulfonic acid) and incubated with Wang and Richard's reagent for 15 min (6 mM dimethyl 3,3'-dithiobispropionimidate, DTBP, Thermo Fisher Scientific, USA). At the same time, cells in an additional plate were counted to ensure equal cell number per sample. DTBP was quenched by 0.03 M Tris-HCl (pH 8) and cells were lysed using modified RIPA buffer. Cell bodies were removed by high-pressure washing and remaining adhesions were collected by scraping. Samples containing isolated IACs were acetone precipitated, dissolved in Laemmli buffer and further processed either for Mass Spectrometry (MS) or Western Blot analysis. Samples were prepared as previously described (Humphries et al., 2009), using a slightly modified procedure. Briefly, samples were loaded onto gradient gels (NuPage 4-12% Bis-Tris protein gels, Thermo Fisher Scientific, UK) and electrophoresis was performed for 3 min (200V). Protein bands were stained with InstantBlue (Expedeon, UK), followed by excision and destaining using series of alternate washing steps with ammonium bicarbonate (Fluka, USA) and acetonitrile (Thermo Fisher Scientific, UK). Washing and drying steps were made in 96-wells perforated plates (GlySci, USA). Gel pieces were dried with acetonitrile and additional drying was performed using vacuum centrifuge. Samples were reduced with dithiothreitol (DTT, 1 hour at 56°C) and alkylated using 55 mM iodoacetamide (37°C, 45 min, dark) (both Sigma-Aldrich, USA). After series of washing and drying steps, gel pieces were incubated with trypsin (1.25 ng/µL, Promega, USA) and incubated for 45 minutes at 4°C, followed by an overnight incubation at 37°C. Peptides were collected and extracted using acetonitrile supplemented with formic acid (Sigma-Aldrich, USA), then dried and resuspended in a solution of 5% (v/v) acetonitrile plus 0.1% (v/v) formic acid. Peptides were desalted using OLIGO R3 beads (Life technologies, USA) using 96-well plates with PVDF membranes (Corning, USA). Desalting was performed with a 0.1% formic acid wash steps before being eluted twice with 50 % acetonitrile in 0.1% formic acid. Peptides were subsequently dried and resuspended in a solution of 5% (v/v) acetonitrile plus 0.1% (v/v) formic acid for LC-MS/MS analysis. Samples were analysed using a modified version of the LC-MS/MS method previously described (Horton et al., 2015). Briefly, an UltiMate® 3000 Rapid Separation LC (RSLC, USA) coupled to an Orbitrap Elite mass detector (Thermo Fisher Scientific, USA) with electrospray ionization. Peptide mixtures were eluted for 44 minutes using a gradient containing 92% of solution A (0.1% formic acid in water) and 8% up to 33% of solution B (0.1% formic acid in acetonitrile). Solvent flow was set to 300 nL per minute. To identify proteins, data were searched against the human Swissprot database (version 2018_01) using Mascot (Matrix science, version 2.5.1). Fragment ion tolerance was set to 0.50 Da, while parent ion tolerance was 5 PPM. Protein identifications were further refined using Scaffold (Proteome software). Protein (99.9%) and peptide (95%) probabilities were assigned using the Protein Prophet algorithm (Nesvizhskii et al., 2003) as incorporated by Scaffold including a minimum of 4 unique peptides per each protein."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Human protein–protein interactions (PPIs) were loaded from STRING database, using stringApp (confidence score cut-off = 0.40, maximum additional interactors = 0) (Doncheva et al., 2019) for Cytoscape software (version 3.7.1) (Shannon et al., 2003). Functional annotation was performed using the Database for annotation, visualization and integrated discovery (DAVID), version 6.8 (Huang da et al., 2009a, Huang da et al., 2009b) and Panther GO database (Thomas et al., 2003). Functional enrichment analysis was carried out using the DAVID_CC subontology list (Benjamini–Hochberg corrected P-value < 0.05, EASE score < 0.1, at least four identified proteins). To summarize gene ontology (GO) terms and visualize them in a similarity-based space, the REVIGO tool was used with the following parameters: comparison of corrected P-values related to GO terms, allowed similarity set to small (0.5), and the Resnik-normalized semantic similarity measure (Supek et al., 2011). Differential protein expression analysis between RPMI-7951 si(-) and RPMI-7951 si(αV) datasets was performed using the QSpec spectral counter tool (Choi et al., 2008). A volcano plot was generated in GraphPad Prism to visualize differentially expressed proteins, using a fold-change threshold of >1.5 (RPMI-7951 si(-) vs. RPMI-7951 si(αV)) and a -log(FDR) >1. Fold changes were calculated based on QSpec output values."],"omics_type":["Proteomics"],"labhead":["Andreja Ambriović-Ristov"],"instrument_platform":[""],"labhead_affiliation":["Laboratory for Cell Biology and Signalling, Division of Molecular Biology, Ruder Boskovic Institute, Zagreb, Croatia"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["nikolina.stojanovic@irb.hr"],"publication":["41776630 Stojanović N, Rac A, Lončarić M, Tadijan A, Paradžik M, Acman M, Humphries JD, Humphries MJ, Ambriović-Ristov A. KANK2 at focal adhesions regulates their maintenance and dynamics, while at fibrillar adhesions it influences cell migration via microtubule-dependent mechanism. Cell Commun Signal. 2026 24(1):224 10.1186/s12964-026-02771-w"],"submitter_affiliation":["Ruđer Bošković Institute"],"submitter_country":["Croatia"],"pubmed_title":["KANK2 at focal adhesions regulates their maintenance and dynamics, while at fibrillar adhesions it influences cell migration via microtubule-dependent mechanism."],"pubmed_authors":["Stojanović Nikolina N, Rac Anja A, Lončarić Marija M, Tadijan Ana A, Paradžik Mladen M, Acman Marta M, Humphries Jonathan D JD, Humphries Martin J MJ, Ambriović-Ristov Andreja A"],"additional_accession":[]},"is_claimable":false,"name":"The melanoma cell line RPMI-7951 adhesome in long-term culture and its comparison to the adhesome upon integrin αV knockdown","description":"Integrins are involved in the metastatic cascade and have been found to be responsible for intrinsic and acquired therapy resistance. Therefore, targeting integrins, or more specifically the signal transduction via integrin adhesion complexes (IACs), is a promising therapeutic opportunity to reduce tumor metastasis and overcome therapeutic resistance. Using mass spectrometry–based proteomics, we analysed the components of integrin adhesion complexes of RPMI-7951 cells in long term culture. The adhesome of RPMI-7951 cells contained three integrin receptor subunits: αV, β5 and β1. The most abundant integrin subunits were αV and β5, suggesting that these cells primarily use αVβ5 for adhesion in long term 2D culture. Integrin subunit α5 was detected, but at very low levels, suggesting that these cells may also express α5β1. To determine which proteins were found in αVβ5-containing adhesions, transient knockdown of integrin subunit αV was performed and IAC composition was compared to cells transfected with control 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