Project description:Transcriptional profiling of mouse HMLEN breast cancer cells (HMLE cells transformed with -Neu oncogene) stably tranduced with pLEX-MCS based lentivirus. Three groups were compared, Vector cells, SNAIL expressing cells; and SNAIL+FBXO11 expressing cells. SNAIL expression induced strong EMT phenotype while SNAIL/FBXO11 reversed cells back to epithelial cells.
Project description:Transcriptional profiling of mouse 4T1 breast cancer cells stably tranduced with pLEX-MCS based lentivirus. Three groups were compared, Vector cells, SNAIL expressing cells; and SNAIL+FBXO11 expressing cells. SNAIL expression induced strong EMT phenotype while SNAIL/FBXO11 reversed cells back to epithelial cells.
Project description:Analysis of four lung cancer cell lines transfected with a vector expressing the transcriptional repressor Snail versus a vector control. Aberrant Snail expression is known to induce an EMT program in lung cancers.
Project description:The main goal of the project was to analyze the effect of SNAIL transcription factor on microRNA expression profile in rhabdomyosarcoma (RMS) cells using the next generation sequencing. Differential expression of microRNAs between three groups was compared in RH30 alveolar RMS cells: WT (WT), shCTRL (modified with control shRNA vector) and shSNAIL (modified with shRNA against SNAIL). Different groups were compared to investigate the effect of SNAIL silencing on microRNA up- or downregulation.
Project description:FBXO11, a member of the F-box protein family, plays a critical role in cellular processes such as protein degradation, cell cycle regulation, and signaling pathways by serving as a substrate recognition component of the SKP1-Cullin-F-box (SCF) ubiquitin ligase complex. Dysregulation of FBXO11 has been implicated in various diseases, including cancer and developmental disorders, yet its full spectrum of interactions and functional roles remains poorly understood. This project aims to perform a comprehensive proteomic profiling of FBXO11-associated protein complexes to uncover its interaction network and better understand its biological functions. Using advanced mass spectrometry-based proteomics, we will identify and characterize the proteins that interact with FBXO11 under different cellular conditions. Additionally, bioinformatics tools will be employed to analyze the identified interactome and explore their functional enrichment in specific pathways and biological processes.