ChiPPI: a novel method for mapping chimeric protein–protein interactions uncovers selection principles of protein fusion events in cancer

Fusion proteins, comprising peptides deriving from the translation of two parental genes, are produced in cancer by chromosomal aberrations. The expressed fusion protein incorporates domains of both parental proteins. Using a methodology that treats discrete protein domains as binding sites for spec...

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Detalles Bibliográficos
Autores: Frenkel-Morgenstern, Milana, Gorohovski, Alessandro, Tagore, Somnath, Sekar, Vaishnovi, Vazquez, Miguel, Valencia, Alfonso|||0000-0002-8937-6789
Tipo de recurso: artículo
Fecha de publicación:2017
País:España
Institución:Universitat Politècnica de Catalunya (UPC)
Repositorio:UPCommons. Portal del coneixement obert de la UPC
Idioma:inglés
OAI Identifier:oai:upcommons.upc.edu:2117/107021
Acceso en línea:https://hdl.handle.net/2117/107021
https://dx.doi.org/10.1093/nar/gkx423
Access Level:acceso abierto
Palabra clave:Protein interactions
Cancer--Alternative treatment--Research
Cancer--Molecular aspects
Signal transduction
Cancer
Fusion protein
Genes
Leukemia
Lymphoma
Oncogene proteins
Parent
Receptor
Epidermal growth factor
Sarcoma
Proton pump inhibitors
Solid tumour
Protein domains
Proteïnes--Anàlisi
Cèl·lules canceroses
Càncer--Aspectes moleculars
Àrees temàtiques de la UPC::Enginyeria biomèdica
Descripción
Sumario:Fusion proteins, comprising peptides deriving from the translation of two parental genes, are produced in cancer by chromosomal aberrations. The expressed fusion protein incorporates domains of both parental proteins. Using a methodology that treats discrete protein domains as binding sites for specific domains of interacting proteins, we have cataloged the protein interaction networks for 11 528 cancer fusions (ChiTaRS-3.1). Here, we present our novel method, chimeric protein–protein interactions (ChiPPI) that uses the domain–domain co-occurrence scores in order to identify preserved interactors of chimeric proteins. Mapping the influence of fusion proteins on cell metabolism and pathways reveals that ChiPPI networks often lose tumor suppressor proteins and gain oncoproteins. Furthermore, fusions often induce novel connections between non-interactors skewing interaction networks and signaling pathways. We compared fusion protein PPI networks in leukemia/lymphoma, sarcoma and solid tumors finding distinct enrichment patterns for each disease type. While certain pathways are enriched in all three diseases (Wnt, Notch and TGF β), there are distinct patterns for leukemia (EGFR signaling, DNA replication and CCKR signaling), for sarcoma (p53 pathway and CCKR signaling) and solid tumors (FGFR and EGFR signaling). Thus, the ChiPPI method represents a comprehensive tool for studying the anomaly of skewed cellular networks produced by fusion proteins in cancer.