scholarly journals MAVS ‐induced mitochondrial membrane remodeling

FEBS Journal ◽  
2019 ◽  
Vol 286 (8) ◽  
pp. 1540-1542 ◽  
Author(s):  
Hector Flores‐Romero ◽  
Ana J. García‐Sáez
FEBS Journal ◽  
2019 ◽  
Vol 286 (8) ◽  
pp. 1543-1560 ◽  
Author(s):  
Ming‐Shih Hwang ◽  
Jérôme Boulanger ◽  
Jonathan D. Howe ◽  
Anna Albecka ◽  
Mathias Pasche ◽  
...  

Author(s):  
Ziyun Yang ◽  
Liang Wang ◽  
Cheng Yang ◽  
Shiming Pu ◽  
Ziqi Guo ◽  
...  

Mitochondria are key regulators of many important cellular processes and their dysfunction has been implicated in a large number of human disorders. Importantly, mitochondrial function is tightly linked to their ultrastructure, which possesses an intricate membrane architecture defining specific submitochondrial compartments. In particular, the mitochondrial inner membrane is highly folded into membrane invaginations that are essential for oxidative phosphorylation. Furthermore, mitochondrial membranes are highly dynamic and undergo constant membrane remodeling during mitochondrial fusion and fission. It has remained enigmatic how these membrane curvatures are generated and maintained, and specific factors involved in these processes are largely unknown. This review focuses on the current understanding of the molecular mechanism of mitochondrial membrane architectural organization and factors critical for mitochondrial morphogenesis, as well as their functional link to human diseases.


Lipids ◽  
2014 ◽  
Vol 49 (7) ◽  
pp. 715-730 ◽  
Author(s):  
Qian Pan ◽  
Min Li ◽  
Yao-Long Shi ◽  
Huwei Liu ◽  
John R. Speakman ◽  
...  

2018 ◽  
Vol 221 (7) ◽  
pp. jeb174458 ◽  
Author(s):  
Dillon J. Chung ◽  
Genevieve C. Sparagna ◽  
Adam J. Chicco ◽  
Patricia M. Schulte

2018 ◽  
Author(s):  
Ming-Shih Hwang ◽  
Jerome Boulanger ◽  
Jonathan Howe ◽  
Anna Albecka ◽  
Mathias Pasche ◽  
...  

Double-stranded RNA (dsRNA) is a potent proinflammatory signature of viral infection. Oligomerization of RIG-I-like receptors on cytosolic dsRNA nucleates self-assembly of the mitochondrial antiviral signaling protein (MAVS). In the current signaling model, the caspase recruitment domains of MAVS form helical fibrils that self-propagate like prions to promote signaling complex assembly. However, there is no conclusive evidence that MAVS forms fibrils in cells or with the transmembrane anchor present. We show here with super-resolution light microscopy that MAVS activation by dsRNA induces mitochondrial membrane remodeling. Quantitative image analysis at imaging resolutions as high as 32 nm shows that in the cellular context MAVS signaling complexes and the fibrils within them are smaller than 80 nm. The transmembrane domain of MAVS is required for its membrane remodeling, interferon signaling and proapoptotic activities. We conclude that membrane tethering of MAVS restrains its polymerization and contributes to mitochondrial remodeling and apoptosis upon dsRNA sensing.


Author(s):  
Krishan K. Arora ◽  
Glenn L. Decker ◽  
Peter L. Pedersen

Hexokinase (ATP: D-hexose 6-phophotransferase EC 2.7.1.1) is the first enzyme of the glycolytic pathway which commits glucose to catabolism by catalyzing the phosphorylation of glucose with ATP. Previous studies have shown diat hexokinase activity is markedly elevated in rapidly growing tumor cells exhibiting high glucose catabolic rates. A large fraction (50-80%) of this enzyme activity is bound to the mitochondrial fraction (1,2) where it has preferred access to ATP (3). In contrast,the hexokinase activity of normal tissues is quite low, with one exception being brain which is a glucose-utilizing tissue (4). Biochemical evidence involving rigorous subfractionation studies have revealed striking differences between the subcellular distribution of hexokinase in normal and tumor cells [See review by Arora et al (4)].In the present report, we have utilized immunogold labeling techniques to evaluate die subcellular localization of hexokinase in highly glycolytic AS-30D hepatoma cells and in the tissue of its origin, i.e., rat liver.


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