Mitochondrial health maintenance in axons

2017 ◽  
Vol 45 (5) ◽  
pp. 1045-1052 ◽  
Author(s):  
Angelika B. Harbauer

Neurons are post-mitotic cells that must function throughout the life of an organism. The high energetic requirements and Ca2+ spikes of synaptic transmission place a burden on neuronal mitochondria. The removal of older mitochondria and the replenishment of the functional mitochondrial pool in axons with freshly synthesized components are therefore important parts of neuronal maintenance. Although the mechanism of mitochondrial protein import and dynamics is studied in great detail, the length of neurons poses additional challenges to those processes. In this mini-review, I briefly cover the basics of mitochondrial biogenesis and proceed to explain the interdependence of mitochondrial transport and mitochondrial health. I then extrapolate recent findings in yeast and mammalian cultured cells to neurons, making a case for axonal translation as a contributor to mitochondrial biogenesis in neurons.

2019 ◽  
Vol 70 (21) ◽  
pp. 6005-6018 ◽  
Author(s):  
Abi S Ghifari ◽  
Shaobai Huang ◽  
Monika W Murcha

Mitochondrial biogenesis requires correct targeting and import of nuclear-encoded proteins to ensure the mitochondrial proteome responds to meet the plant’s energetic demands. Protein-degrading machineries also play key roles in protein import and mitochondrial biogenesis.


2020 ◽  
Vol 401 (6-7) ◽  
pp. 645-661 ◽  
Author(s):  
Maria Clara Avendaño-Monsalve ◽  
José Carlos Ponce-Rojas ◽  
Soledad Funes

AbstractMitochondrial protein import is one of the key processes during mitochondrial biogenesis that involves a series of events necessary for recognition and delivery of nucleus-encoded/cytosol-synthesized mitochondrial proteins into the organelle. The past research efforts have mainly unraveled how membrane translocases ensure the correct protein sorting within the different mitochondrial subcompartments. However, early steps of recognition and delivery remain relatively uncharacterized. In this review, we discuss our current understanding about the signals on mitochondrial proteins, as well as in the mRNAs encoding them, which with the help of cytosolic chaperones and membrane receptors support protein targeting to the organelle in order to avoid improper localization. In addition, we discuss recent findings that illustrate how mistargeting of mitochondrial proteins triggers stress responses, aiming to restore cellular homeostasis.


1998 ◽  
Vol 274 (5) ◽  
pp. C1380-C1387 ◽  
Author(s):  
Mark Takahashi ◽  
Alan Chesley ◽  
Damien Freyssenet ◽  
David A. Hood

We previously demonstrated that subsarcolemmal (SS) and intermyofibrillar (IMF) mitochondrial subfractions import proteins at different rates. This study was undertaken to investigate 1) whether protein import is altered by chronic contractile activity, which induces mitochondrial biogenesis, and 2) whether these two subfractions adapt similarly. Using electrical stimulation (10 Hz, 3 h/day for 7 and 14 days) to induce contractile activity, we observed that malate dehydrogenase import into the matrix of the SS and IMF mitochondia isolated from stimulated muscle was significantly increased by 1.4- to 1.7-fold, although the pattern of increase differed for each subfraction. This acceleration of import may be mitochondrial compartment specific, since the import of Bcl-2 into the outer membrane was not affected. Contractile activity also modified the mitochondrial content of proteins comprising the import machinery, as evident from increases in the levels of the intramitochondrial chaperone mtHSP70 as well as the outer membrane import receptor Tom20 in SS and IMF mitochondria. Addition of cytosol isolated from stimulated or control muscles to the import reaction resulted in similar twofold increases in the ability of mitochondria to import malate dehydrogenase, despite elevations in the concentration of mitochondrial import-stimulating factor within the cytosol of chronically stimulated muscle. These results suggest that chronic contractile activity modifies the extra- and intramitochondrial environments in a fashion that favors the acceleration of precursor protein import into the matrix of the organelle. This increase in protein import is likely an important adaptation in the overall process of mitochondrial biogenesis.


2000 ◽  
Vol 276 (3) ◽  
pp. 1028-1034 ◽  
Author(s):  
Khaleque Md. Abdul ◽  
Kazutoyo Terada ◽  
Masato Yano ◽  
Michael T. Ryan ◽  
Illo Streimann ◽  
...  

FEBS Journal ◽  
2005 ◽  
Vol 272 (19) ◽  
pp. 5031-5055 ◽  
Author(s):  
Ludovic Mercy ◽  
Aurélia de Pauw ◽  
Laetitia Payen ◽  
Silvia Tejerina ◽  
Andrée Houbion ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document