Akademik Veri Yönetim Sistemi
Başbınar Y. (Yürütücü), Ellidokuz E.
Yükseköğretim Kurumları Destekli Proje, 2021 - 2024
Revealing the genes that have been shown to be effective in the protein
degradation process and the molecular mechanisms and pathways associated with
them will enable the provision of biomarkers and the elucidation of therapeutic targets.
Ubiquitin plays a role in many processes such as apoptosis, cell division and
proliferation, cell degeneration, DNA transcription and repair, immune response,
organelle biogenesis, antigen processes, receptor modulation, viral infections by
binding to proteins. E1 (activating enzyme), E2 (conjugating enzyme) and E3 (ligase)
enzymes that control binding as well as de-ubiquitination (DUB) enzymes that control
dissociation are involved in ubiquitin modification of proteins. Recently, an increasing
number of studies have been published on the association between altered expression
or germline/somatic mutations of DUB enzymes and many cancers. There are some
studies showing the association of DUB enzymes with EMT as well as many processes
related to tumor metastasis. The aim of the study is to interrogate the protein turnover
rate (ribosome-proteasome pathways) as a new drug target in colorectal cancer from
transcriptome gene expression data and to create a profile target by validating it with
in-silico bioinformatics methods. Genes related to the ubiquitin-proteasome pathway
(UPP) were compiled from previous studies and a ubiquitin-proteasome pathwayspecific
network was created with protein interactions. The network was analyzed and
drug targets were found for ADRB2, RXRA, CHRNA1, and FGFR2.
Key words: Novel drug targets, in-silico analysis, ubiquitin-proteasome
pathway genes, gene network construction, differential gene expression analysis, gene
set enrichment analysis.