IDENTIFYING ROLE OF YB1 AND NPM1 AS PART OF HISTONE 3 MUTANT PROTEIN INTERACTOME, IN H3 MUTATED PHGG

Abstract AIMS Paediatric high-grade gliomas (pHGG) are the leading cause of childhood cancer deaths, accounting for over 40% deaths in UK. pHGG tumours harbour histone H3 mutations, defining 50% cases. Studies show prominent mutations as being H3.3K27M and H3.3G34R/V. Our previous research has identified unique common interacting binding partners H3-G34R H3-G34V mutant proteins. Among these we have focused on YB-1 Nucleophosmin (NPM1). is multifunctional transcription factor a well-known oncogenic protein. NPM1 molecular chaperone frequently over- expressed well. aim to analyse role mutated pHGG, order identify targeted therapeutic option diffcult treat tumours. METHOD Further data analyses mass spectrometric proteomic were performed. Subsequently, glioma cell lines, control wild type cells cultured then subjected analyses. A comparative immunofluorescence microscopy, western blot performed investigate NPM-1. RESULTS Results verified further showed altered protein expression localization pHGG. CONCLUSIONS study support that important proteins H3G34-mutated pHGGs can be explored targets