Mitochondrial biogenesis is dependant of transcription factors such as nuclear STO-609 acetate respiratory factors and TAK 960 hydrochloride estrogen-related receptors that coordinate the synthesis of OXPHOS complex subunits encoded by the nuclear and mitochondrial genomes. The transcriptional efficiency of these factors is controlled by coactivators from the peroxisome proliferator-activated receptor c coactivator-1 family, i.e., PGC-1a, PGC-1b and the PGC-1-related coactivator, that integrates mitochondrial biogenesis and function to various environmental signals. We previously showed that the ubiquitous PRC member was able to control mitochondrial fission by modulating the Fission-1 expression level in cancer cells, in addition to its effect on mitochondrial biogenesis. Numerous studies have highlighted selected miRNAs related to glioma pathogenesis. Some of them have potential applications as novel diagnostic and prognostic indicators. Thus, the reexpression of miR-34a encoded at Chr1p36.22, a region deleted in many glioblastomas, could be associated with reduced tumor proliferation, cell migration and invasion. Conversely, miR- 21 has been identified as an anti-apoptotic factor and presents a significant up-regulation in glioblastoma, while its inhibition induced apoptosis in glioblastoma cells in vitro and in vivo. This miRNA is involved in the down regulation of the tumor suppressor gene PTEN, in caspase 3/7 activation and confers a drug resistance to cancer cells. Moreover, an over-expression of miR-221 has been linked with increased cellular proliferation and an over-expression of the c-KIT gene. These miRNAs have also recently been related to a pool of miRNAs called mitomiRs, which are associated with the mitochondrial compartment. Their role in the control of mitochondrial functions and cell redox status is now established. In this study, we focused on the role for MTAs in the OXPHOS process and the dynamics of mitochondrial networks. For this purpose, we used the T98G cellular model of human glioblastoma, in which we have previously demonstrated the incorporation and cytoskeleton effect for 10 mM NFL-TBS.40-63 peptide. Previously, we have shown that T98G human glioblastoma cells internalized the NFL-TBS.40-63 peptide at a 10 mM concentration, which induces the disruption of their microtubule network. Consequently, tubulin is aggregated around the nucleus, while cells lose their extensions and become spherical. Using markers of both mitochondrial and microtubule networks, in association with a marked peptide, confocal microscopy showed that the peptide entered in T98G and accumulated in a polarized manner.