scholarly journals Serine 392 phosphorylation modulates p53 mitochondrial translocation and transcription-independent apoptosis

2017 ◽  
Vol 25 (1) ◽  
pp. 190-203 ◽  
Author(s):  
Cédric Castrogiovanni ◽  
Béranger Waterschoot ◽  
Olivier De Backer ◽  
Patrick Dumont
Keyword(s):  
Mitochondrial Translocation ◽  
Serine 392

197-OR: IL-6 Protects Pancreatic ß Cells from Oxidative Stress via NRF2 Mitochondrial Translocation and Mitophagy

Diabetes ◽  
2019 ◽  
Vol 68 (Supplement 1) ◽  
pp. 197-OR
Author(s):  
MICHELLE MARASCO ◽  
ABASS M. CONTEH ◽  
CHARANYA MURALIDHARAN ◽  
ELIZABETH PFEIFER ◽  
AMELIA K. LINNEMANN
Keyword(s):  
Oxidative Stress ◽  
Mitochondrial Translocation

scholarly journals Mitochondrial Uncoupling Inhibits p53 Mitochondrial Translocation in TPA-Challenged Skin Epidermal JB6 Cells

PLoS ONE ◽  
2010 ◽  
Vol 5 (10) ◽  
pp. e13459 ◽  
Author(s):  
Fei Wang ◽  
Xueqi Fu ◽  
Xia Chen ◽  
Xinbin Chen ◽  
Yunfeng Zhao
Keyword(s):  
Mitochondrial Uncoupling ◽  
Mitochondrial Translocation ◽  
Jb6 Cells

Mitochondrial Translocation of TFEB Regulates Complex I and Inflammation

2021 ◽  
Author(s):  
Chiara Calabrese ◽  
Hendrik Nolte ◽  
Melissa Pitman ◽  
Philipp Lampe ◽  
Raymond Laboy ◽  
...  
Keyword(s):  
Complex I ◽  
Mitochondrial Translocation

scholarly journals The Pam18/Tim14-Pam16/Tim16 complex of the mitochondrial translocation motor: The formation of a stable complex from marginally stable proteins

2006 ◽  
Vol 16 (2) ◽  
pp. 316-322 ◽  
Author(s):  
O. Iosefson ◽  
R. Levy ◽  
M. Marom ◽  
O. Slutsky-Leiderman ◽  
A. Azem
Keyword(s):  
Stable Complex ◽  
Mitochondrial Translocation

scholarly journals Increased long noncoding RNA maternally expressed gene 3 contributes to podocyte injury induced by high glucose through regulation of mitochondrial fission

2020 ◽  
Vol 11 (9) ◽  
Author(s):  
Qiongxia Deng ◽  
Ruowei Wen ◽  
Sirui Liu ◽  
Xiaoqiu Chen ◽  
Shicong Song ◽  
...  
Keyword(s):  
High Glucose ◽  
Noncoding Rna ◽  
Diabetic Kidney Disease ◽  
Mitochondrial Fission ◽  
Diabetic Mice ◽  
Podocyte Injury ◽  
Mitochondrial Translocation ◽  
Maternally Expressed Gene 3

Abstract Excessive mitochondrial fission plays a key role in podocyte injury in diabetic kidney disease (DKD), and long noncoding RNAs (lncRNAs) are important in the development and progression of DKD. However, lncRNA regulation of mitochondrial fission in podocytes is poorly understood. Here, we studied lncRNA maternally expressed gene 3 (Meg3) in mitochondrial fission in vivo and in vitro using human podocytes and Meg3 podocyte-specific knockdown mice. Expression of lncRNA Meg3 in STZ-induced diabetic mice was higher, and correlated with the number of podocytes. Excessive mitochondrial fission of podocytes and renal histopathological and physiological parameters were improved in podocyte-specific Meg3 knockdown diabetic mice. Elongated mitochondria with attenuated podocyte damage, as well as mitochondrial translocation of dynamin-related protein 1 (Drp1), were decreased in Meg3 knockout podocytes. By contrast, increased fragmented mitochondria, podocyte injury, and Drp1 expression and phosphorylation were observed in lncRNA Meg3-overexpressing podocytes. Treatment with Mdivi1 significantly blunted more fragmented mitochondria and reduced podocyte injury in lncRNA Meg3-overexpressing podocytes. Finally, fragmented mitochondria and Drp1 mitochondrial translocation induced by high glucose were reduced following treatment with Mdivi1. Our data show that expression of Meg3 in podocytes in both human cells and diabetic mice was higher, which regulates mitochondrial fission and contributes to podocyte injury through increased Drp1 and its translocation to mitochondria.

scholarly journals Cyclovirobuxine D Induces Apoptosis and Mitochondrial Damage in Glioblastoma Cells Through ROS-Mediated Mitochondrial Translocation of Cofilin

2021 ◽  
Vol 11 ◽  
Author(s):  
Lin Zhang ◽  
Ruoqiu Fu ◽  
Dongyu Duan ◽  
Ziwei Li ◽  
Bin Li ◽  
...  
Keyword(s):  
Cell Lines ◽  
Oxidant Stress ◽  
Mitochondrial Damage ◽  
Dependent Manner ◽  
Mitochondrial Translocation ◽  
Mitochondrial Superoxide ◽  
Human Astrocytes ◽  
Anti Cancer ◽  
Normal Human ◽  
Induced Apoptosis

BackgroundCyclovirobuxine D (CVBD), a steroidal alkaloid, has multiple pharmacological activities, including anti-cancer activity. However, the anti-cancer effect of CVBD on glioblastoma (GBM) has seldom been investigated. This study explores the activity of CVBD in inducing apoptosis of GBM cells, and examines the related mechanism in depth.MethodsGBM cell lines (T98G, U251) and normal human astrocytes (HA) were treated with CVBD. Cell viability was examined by CCK-8 assay, and cell proliferation was evaluated by cell colony formation counts. Apoptosis and mitochondrial superoxide were measured by flow cytometry. All protein expression levels were determined by Western blotting. JC-1 and CM-H2DCFDA probes were used to evaluate the mitochondrial membrane potential (MMP) change and intracellular ROS generation, respectively. The cell ultrastructure was observed by transmission electron microscope (TEM). Colocalization of cofilin and mitochondria were determined by immunofluorescence assay.ResultsCVBD showed a greater anti-proliferation effect on the GBM cell lines, T98G and U251, than normal human astrocytes in dose- and time-dependent manners. CVBD induced apoptosis and mitochondrial damage in GBM cells. We found that CVBD led to mitochondrial translocation of cofilin. Knockdown of cofilin attenuated CVBD-induced apoptosis and mitochondrial damage. Additionally, the generation of ROS and mitochondrial superoxide was also induced by CVBD in a dose-dependent manner. N-acetyl-L-cysteine (NAC) and mitoquinone (MitoQ) pre-treatment reverted CVBD-induced apoptosis and mitochondrial damage. MitoQ pretreatment was able to block the mitochondrial translocation of cofilin caused by CVBD.ConclusionsOur data revealed that CVBD induced apoptosis and mitochondrial damage in GBM cells. The underlying mechanism is related to mitochondrial translocation of cofilin caused by mitochondrial oxidant stress.

scholarly journals BimS-induced apoptosis requires mitochondrial localization but not interaction with anti-apoptotic Bcl-2 proteins

2007 ◽  
Vol 177 (4) ◽  
pp. 625-636 ◽  
Author(s):  
Arnim Weber ◽  
Stefan A. Paschen ◽  
Klaus Heger ◽  
Florian Wilfling ◽  
Tobias Frankenberg ◽  
...  
Keyword(s):  
Mutational Analysis ◽  
Membrane Insertion ◽  
Apoptosis Induction ◽  
Mitochondrial Targeting ◽  
Mitochondrial Localization ◽  
Mitochondrial Translocation ◽  
Killing Activity ◽  
Regulated Expression ◽  
Direct Binding ◽  
Induced Apoptosis

Release of apoptogenic proteins such as cytochrome c from mitochondria is regulated by pro- and anti-apoptotic Bcl-2 family proteins, with pro-apoptotic BH3-only proteins activating Bax and Bak. Current models assume that apoptosis induction occurs via the binding and inactivation of anti-apoptotic Bcl-2 proteins by BH3-only proteins or by direct binding to Bax. Here, we analyze apoptosis induction by the BH3-only protein BimS. Regulated expression of BimS in epithelial cells was followed by its rapid mitochondrial translocation and mitochondrial membrane insertion in the absence of detectable binding to anti-apoptotic Bcl-2 proteins. This caused mitochondrial recruitment and activation of Bax and apoptosis. Mutational analysis of BimS showed that mitochondrial targeting, but not binding to Bcl-2 or Mcl-1, was required for apoptosis induction. In yeast, BimS enhanced the killing activity of Bax in the absence of anti-apoptotic Bcl-2 proteins. Thus, cell death induction by a BH3-only protein can occur through a process that is independent of anti-apoptotic Bcl-2 proteins but requires mitochondrial targeting.

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