Proteomics

Dataset Information

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Dynamics of Mitochondrial Proteome and Acetylome in Glioblastoma Cells with Contrasting Metabolic Phenotypes


ABSTRACT: The dysregulated energy metabolism of glioblastoma cells is a critical factor in tumor development and progression. Lysine acetylation, regulated by the mitochondrial enzyme SIRT3, is known to play a key role in the metabolic phenotype of glioblastoma. To better understand how SIRT3 regulates mitochondrial metabolism, we inhibited SIRT3 and examined the proteome and acetylome of two glioblastoma cell lines with different metabolic preferences. Our results indicate that protein synthesis machineries are regulated by lysine acetylation and play a role in the metabolic phenotype. We also identified new SIRT3 targets that have not been previously associated with specific functions, highlighting their potential as future targets for further study. These findings enhance our understanding of the complex regulation of energy metabolism in glioblastoma and provide potential targets for future therapies.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture

DISEASE(S): Brain Glioblastoma Multiforme

SUBMITTER: Diana Lashidua Fernandez Coto  

LAB HEAD: Sergio Manuel Encarnacion Guevara

PROVIDER: PXD045197 | Pride | 2024-05-23

REPOSITORIES: Pride

Dataset's files

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20200702_JG_1_R1.raw Raw
20200702_JG_1_R1a.raw Raw
20200702_JG_1_R2.raw Raw
20200702_JG_2_R1.raw Raw
20200702_JG_2_R1a.raw Raw
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Publications

Dynamics of Mitochondrial Proteome and Acetylome in Glioblastoma Cells with Contrasting Metabolic Phenotypes.

Fernández-Coto Diana Lashidua DL   Gil Jeovanis J   Ayala Guadalupe G   Encarnación-Guevara Sergio S  

International journal of molecular sciences 20240319 6


Glioblastoma, a type of cancer affecting the central nervous system, is characterized by its poor prognosis and the dynamic alteration of its metabolic phenotype to fuel development and progression. Critical to cellular metabolism, mitochondria play a pivotal role, where the acetylation of lysine residues on mitochondrial enzymes emerges as a crucial regulatory mechanism of protein function. This post-translational modification, which negatively impacts the mitochondrial proteome's functionality  ...[more]

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