AI Article Synopsis
- The adenine nucleotide translocator (ANT) plays a key role in several important cellular processes, such as energy supply, maintaining mitochondrial DNA, and regulating programmed cell death (apoptosis).
- The paper discusses six different structures of ANT1, noting that changes in these structures are influenced by the cell's energy needs and help manage oxidative phosphorylation (OXPHOS) activity.
- It further reveals that under low respiratory chain activity, the pro-apoptotic protein Bax can trigger a significant release of cytochrome c from specific ANT1 structures, highlighting the connection between ANT’s structural changes and apoptosis depending on energy levels.
Article Abstract
The adenine nucleotide translocator (ANT) is a control point of several fundamental cell processes, as diverse as cell energy supply, mitochondrial DNA maintenance, and apoptosis. This paper describes six individual structures of the carrier, distinguished according to ANT1 oligomeric and conformational states, as well as associations with other proteins. Transitions between these structures depend on energy demand and thus contribute to a metabolic reserve of oxidative phosphorylation (OXPHOS) activity. Moreover, at low respiratory chain activity, we demonstrate that, unlike a mitochondrial Ca2+ upload, Bax, a pro-apoptotic Bcl-2-family protein, is able to trigger a massive release of cytochrome c from one of these ANT1 structures. These new insights emphasize the close relationship between structural rearrangements of ANT and molecular apoptotic events at distinct cell energy levels. OXPHOS functioning has to therefore be considered a crucial control point for the events leading to these contrasting pathways.
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| http://dx.doi.org/10.2741/e255 | DOI Listing |
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