{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2020/05/PXD017644/ROC-ssTrypAspNLocalPeptide.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2020/05/PXD017644/ROC-igfTrypAspNLocalPeptide.xlsx"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2020/05/PXD017644/GeraldineKelly-077_2012.pptx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2020/05/PXD017644/GK-ROC-2-LocalDB-120201.htm","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2020/05/PXD017644/GK-ROC-3-LocalDB-120201.htm","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2020/05/PXD017644/GK-ROC-1-LocalDB-120201.htm"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["r.oconnor@ucc.ie"],"submitter":["Rosemary O'Connor"],"technology_type":["Mass Spectrometry","Gel-based experiment"],"software":["Not available"],"submitter_keywords":["Tyr1136","Tyr1131","Igf-1","Tyr125051","Tyr1135","Igf-1 receptor"],"full_dataset_link":["http://www.ebi.ac.uk/pride/archive/projects/PXD017644"],"tissue":["Cell Culture","Fibroblast"],"sample_protocol":["Mass Spectrometry for phospho-peptide mapping of the IGF-1R was done at the FingerPrints Proteomics Facility the University of Dundee. IGF-1R was immunoprecipitated from R- cells transfected with pcDNA3 IGF-1R WT and that were either serum-starved or stimulated with IGF-1 were transferred as protein G agarose-bound protein precipitates to the Dundee facility where they were subjected to Trypsin/AspN digestion and enrichment of phosphor-peptides by titanium dioxide. Mass Spectrometry was performed using an Orbitrap Velos system."],"repository":["Pride"],"quantification_method":["emPAI"],"modification":["phosphorylated residue"],"data_protocol":["Data analysis were initially processed at the FingerPrints Proteomics Facility the University of Dundee. The peaks were analysed for the enriched peptide, EVSFYYSEENKLPEPEEL , using the Thermo Xcaliber Qual Browser. Mascot search results were converted to an excel file."],"omics_type":["Proteomics"],"labhead":["Rosemary O'Connor"],"instrument_platform":["LTQ Orbitrap Velos"],"labhead_affiliation":["School of Biochemistry and Cell Biology, University College Cork, Cork, Ireland"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["32457113 Rieger L, O'Shea S, Godsmark G, Stanicka J, Kelly G, O'Connor R. IGF-1 receptor activity in the Golgi of migratory cancer cells depends on adhesion-dependent phosphorylation of Tyr1250 and Tyr1251. Sci Signal. 2020 13(633) 10.1126/scisignal.aba3176"],"submitter_mail":["r.oconnor@ucc.ie"],"submitter_affiliation":["University College Cork"],"submitter_country":["Ireland"],"pubmed_abstract":["Although insulin-like growth factor 1 (IGF-1) signaling promotes tumor growth and cancer progression, therapies that target the IGF-1 receptor (IGF-1R) have shown poor clinical efficacy. To address IGF-1R activity in cancer cells and how it differs from that of the closely related insulin receptor (IR), we focused on two tyrosines in the IGF-1R C-terminal tail that are not present in the IR and are essential for IGF-1-mediated cancer cell survival, migration, and tumorigenic growth. We found that Tyr1250 and Tyr1251 (Tyr1250/1251) were autophosphorylated in a cell adhesion-dependent manner. To investigate the consequences of this phosphorylation, we generated phosphomimetic Y1250E/Y1251E (EE) and nonphosphorylatable Y1250F/Y1251F (FF) mutant forms of IGF-1R. Although fully competent in kinase activity and signaling, the EE mutant was more rapidly internalized and degraded than either the wild-type or FF receptor. IGF-1 promoted the accumulation of wild-type and EE IGF-1R within the Golgi apparatus, whereas the FF mutant remained at the plasma membrane. Golgi-associated IGF-1R signaling was a feature of migratory cancer cells, and Golgi disruption impaired IGF-1-induced signaling and cell migration. Upon the formation of new cell adhesions, IGF-1R transiently relocalized to the plasma membrane from the Golgi. Thus, phosphorylation at Tyr1250/1251 promoted IGF-1R translocation to and signaling from the Golgi to support an aggressive cancer phenotype. This process distinguishes IGF-1R from IR signaling and could contribute to the poor clinical efficacy of antibodies that target IGF-1R on the cell surface."],"pubmed_title":["IGF-1 receptor activity in the Golgi of migratory cancer cells depends on adhesion-dependent phosphorylation of Tyr1250 and Tyr1251."],"pubmed_authors":["Rieger Leonie L, O'Shea Sandra S, Godsmark Grant G, Stanicka Joanna J, Kelly Geraldine G, O'Connor Rosemary R"],"sample_synonyms":["Plantar Prints, Plantar Print, Peptidomics, Blood, Sepharose C1 4B, Phosphor, brookite, Print, protein, Spectrum Analyses, Serum, protein-containing complex, peptide, Polypeptides, nano-TiO2, protein polypeptide chains, peptido, polypeptide chain, anatase, Mass, titanium white, system, Fingerprinting, Analysis, protein aggregate, fosforo, Mass Spectroscopy, CD221, Mass Spectrum Analysis, igf-1r, Slrr1c, Sepharose, Fingerprints, anatomical systems, peptides, Analyses, xigf1r, Titania, P, beta-Trypsin, somatomedin-C, proteins, food additive E171, phosphore, igf-1, rutile, C1 4B, Phosphorus, IGF1, 6-anhydro-alpha-L-galactopyranosyl-(1->3)-beta-D-galactopyranan, xigf1, Agarose, Peptide Fingerprint, nano-anatase, C730016P09Rik, peptidos, Plantar, 6-An-alpha-L-Galp-(1->3)-beta-D-Galp-(1->]n, Prints, IGF-I, Mapping, protein complex, 4B, Igf-I, somatomedin, Peptide Fingerprinting, titanium oxide, IBP1, Blood Serum, igf1-A, Spectrum Analysis, Protein Fingerprints, Peptide, Cell, phosphorus, Spectroscopy, Fingerprint, polypeptide, native protein, natural protein, body system., [4)-3, 15P, mechano growth factor, Protein, hyft, Sepharose C1, A330103N21Rik, D930020L01, University, 4631401G09Rik, connected anatomical system, Igf-1, Mass Spectrum Analyses, SLRR1C, Protein Fingerprinting, Mass Spectrum, OS3, anatase titanium dioxide, Aspn, Spectrometry, Tripcellim, Peptide Fingerprints, (1->4)-3, beta Trypsin, IGF-1R, PLAP-1, Plap1, organ system, Protein Fingerprint, Trypure, AA986886, PLAP1, MGF, Sepharose 4B, Peptid, Polypeptide, Serums"],"pubmed_title_synonyms":["malignant Growth, IGF-I, malignancy, endocytic receptor activity, malignant, FON1, cell type cancer, Igf-I, 2-Amino-3-(p-hydroxyphenyl)propionic acid, transport receptor activity, Phosphorylations, somatomedin, Golgi complex, SUPERMAN, Synaptosomal-associated 25 kDa protein, IBP1, FLORAL ORGAN NUMBER 1, igf1-A, signalling receptor activity, Cell, phosphorylation, Tyrosine, OCA1A, MT, tirosina, skc35, mechano growth factor, malignant neoplasm (disease), organ system cancer, SUP, receptor activity involved in signal transduction, GENA70, Igf-1, neoplasm, tyrosine, malignant tumour, OCAIA, SHEP3, primary cancer, neoplasm (disease), 2-amino-3-(4-hydroxyphenyl)propanoic acid, 3-(p-Hydroxyphenyl)alanine, Bdr, somatomedin-C, albino, FLO10, FLORAL DEFECTIVE 10., Y, Super protein, Golgi, HERP, igf-1, malignant tumor, sp, CA, SNAP-25, Golgi ribbon, c, Mif1, receptor activity, viral antireceptor activity, malignant neoplasm, malignant neoplastic disease, CMM8, IGF1, Tyr, MGF, xigf1, receptor guanylate cyclase activity, C730016P09Rik, Tyrosin, receptor activity involved in receptor-mediated endocytosis, cancer, FLORAL DEFECTIVE 10"],"data_synonyms":["Plantar Prints, Fingerprints, results., Plantar Print, peptides, Analyses, Peptidomics, AW549739, Print, MASCOT, Peptide, Lccp, Fingerprint, polypeptide, peptide, mKIAA0989, Polypeptides, ClvPrd, peptido, Data, Peptid, peptidos, Plantar, University, Polypeptide, Analysis, Data Analyses, Prints, C79691"],"description_synonyms":["malignant Growth, IGF-I, malignancy, biological signaling, region or site annotation, malignant, cell type cancer, postnatal development, Igf-I, somatomedin, growth and development, IBP1, Tumor, Viabilities, insulin-like growth factor, igf1-A, uroptérygie, Cell, binding site, CD220, Cell Viabilities, development, Readability, MT, IR, insulin-like growth factor receptor ligand, mechano growth factor, malignant neoplasm (disease), Survival, hyft, organ system cancer, A330103N21Rik, D930020L01, single organism cell adhesion, IGF receptor binding, Igf-1, neoplasm, malignant tumour, region, Viability, CD221, igf-1r, study, positional, primary cancer, positional polypeptide feature, tail fin, growth pattern, xigf1r, non-developmental growth, INSDC_feature:misc_binding, caudal subdivision, Tails, neoplasm (disease), postnatal growth, nageoire caudale, somatomedin-C, Cell Adhesions, present in organism, Understanding, uroptère, igf-1, malignant tumor, IGF-1R, signalling, CA, Adhesions, INSR, tail, signalling process, binding_or_interaction_site, malignant neoplasm, malignant neoplastic disease, IGF1, signaling process, MGF, xigf1, Adhesion, cell adhesion molecule activity., site, C730016P09Rik, growth, cancer, Cell Viability, single organism signaling"],"pubmed_abstract_synonyms":["projections, malignant Growth, Forms, Activity, FON1, Feature, postnatal development, Addresses, A4, growth and development, sci, Tumor, Viabilities, FLORAL ORGAN NUMBER 1, phosphorylation, CD220, dysfunctional, dmTAF[[II]]230, insulin-like growth factor receptor ligand, skc35, SUP, HOW, How, IGF receptor binding, phosphokinase activity, l(3)j5D5, Viability, multicellular organismal biosynthetic process, CD221, 24B, igf-1r, single-organism biosynthetic process, tail fin, TFIID TAF250, cel, anabolism, neoplasm (disease), 2-amino-3-(4-hydroxyphenyl)propanoic acid, 3-(p-Hydroxyphenyl)alanine, nageoire caudale, Bdr, somatomedin-C, stru, present in organism, l(3)S053606, uroptère, Y, Super protein, Golgi, CG10293, sp, CA, SNAP-25, inner endospore membrane, l(3)j5B5, c, Adhesions, plasma membrane lipid bilayer, INSR, tail, malignant neoplasm, IGF1, plasmalemma, signaling process, Tyr, papilla, xigf1, Adhesion, C730016P09Rik, associated, TL, single organism signaling, IGF-I, malignancy, 0904/17, dTAF[[II]]230, anatomical protrusion, Igf-I, 2-Amino-3-(p-hydroxyphenyl)propionic acid, lamina, TAF200, somatomedin, flanges, IBP1, TAFII-250, insulin-like growth factor, igf1-A, TAF250/230, antibodies, uroptérygie, partial functionality, Tyrosine, cellular membrane, TAFII250, juxtamembrane, SZ1, mechano growth factor, organ system cancer, shelf, GENA70, A330103N21Rik, D930020L01, bacterial inner membrane, Igf-1, tyrosine, OCAIA, SHEP3, cell membrane, growth pattern, Golgi Complex, non-developmental growth, Tails, shelves, pooled, lacks function of type, Features, CG17603, TAF[[II]], projection, ridge, low functionality, Phenotypes, cell associated., DMDA, Taf250, spine, SR3-5, anon-EST:Liang-2.39, cancer, cell bound, TAF230, FLORAL DEFECTIVE 10, biological signaling, d230, lamellae, P62, cell type cancer, impaired, dTAFII250, SUPERMAN, biosynthesis, EfW1, process of organ, TYPE, protrusion, DAGA4, lamella, IR, dmTAF1, Taf230, Survival, single organism cell adhesion, MAM, neoplasm, SCG3, malignant tumour, TAF250, Taf200, dTAF[[II]]250, l(3)s2612, formation, xigf1r, cell, cell adhesion molecule activity, Complex, dysfunction, albino, Taf1p, ridges, igf-1, synthesis, dTAF250, Mif1, Golgi ribbon, CMM8, DmelCG10293, Characteristics, Tyrosin, TAF, laminae, integral to plasma membrane, TAF[[II]]250, clone 2.39, malignant, integral component of plasma membrane, anatomical process, Phosphorylations, l(3)84Ab, Golgi complex, Synaptosomal-associated 25 kDa protein, BG:DS00004.13, qkr, l(3)S090417, Apparatus, Cell, LGMD2C, dTAF230, Cell Viabilities, development, OCA1A, MT, Characteristic, tirosina, p230, malignant neoplasm (disease), KH93F, hyft, TAF[[II]]250/230, TFIID, flange, organ process, who, Taf[[II]]250, primary cancer, TAF[[II]]230, DMDA1, caudal subdivision, postnatal growth, Cell Adhesions, FLO10, TAF[II]250, Who/How, HERP, malignant tumor, IGF-1R, signalling, processes, process, having decreased function, DmelCG17603, signalling process, malignant neoplastic disease, MGF, SCARMD2, qkr[93F], processus, cytoplasmic membrane, growth, Cell Viability, General activity, TAF1"],"name_synonyms":["IGF-I, igf-1., IGF1, MGF, mechano growth factor, xigf1, Igf-I, Phosphorylations, somatomedin-C, somatomedin, C730016P09Rik, IBP1, Igf-1, igf1-A, phosphorylation"],"additional_accession":[]},"is_claimable":false,"name":"Identification of phosphorylation sites in the IGF-1 Receptor","description":"Although Insulin-like Growth Factor (IGF-1) signaling promotes tumor growth and cancer progression, IGF-1 Receptor-targeted therapies have shown poor clinical efficacy. The mechanistic basis for this is unclear as is our understanding of what distinguishes IGF-1R signaling from the closely related Insulin receptor (IR) signaling. This study illuminates both issues. A site in the IGF-1R C-terminal tail incorporating two tyrosines that are not present in the Insulin receptor (IR) was previously shown to be essential for IGF-1-mediated cancer cell survival, migration and tumorigenic growth. Here, we establish that the Y1250/Y1251 site is autophosphorylated in a cell adhesion-dependent 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