Unveiling the impact of SUMOylation at K298 site of heat shock factor 1 on glioblastoma malignant progression.

ABSTRACT:

Background

Glioblastoma (GBM) poses a significant medical challenge due to its aggressive nature and poor prognosis. Mitochondrial unfolded protein response (UPRmt) and the heat shock factor 1 (HSF1) pathway play crucial roles in GBM pathogenesis. Post-translational modifications, such as SUMOylation, regulate the mechanism of action of HSF1 and may influence the progression of GBM. Understanding the interplay between SUMOylation-modified HSF1 and GBM pathophysiology is essential for developing targeted therapies.

Methods

We conducted a comprehensive investigation using cellular, molecular, and in vivo techniques. Cell culture experiments involved establishing stable cell lines, protein extraction, Western blotting, co-immunoprecipitation, and immunofluorescence analysis. Ma

SUBMITTER: Li X 

PROVIDER: S-EPMC11415976 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature