ArticlemicroPublication biology2026
The N-terminal α helix domain of the mitochondrial VDAC protein Por2 is dispensable for promoting the nuclear localization of yeast AMPK.
Article in microPublication biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
In yeast, the mitochondrial voltage-dependent anion channel (VDAC) proteins Por1 and Por2 play regulatory roles in the regulation of Snf1, an ortholog of AMP-activated protein kinase (AMPK). An important question is whether Por1 and Por2 serve as Snf1-coupled energy sensors. VDACs are β-barrel proteins, but they have a flexibly-linked N-terminal α helix (NAH) domain, suggesting a possible role in Snf1 signaling. Here, we asked whether the NAH domain of Por2 is required for promoting Snf1 nuclear translocation. In our experimental setup, the Por2 NAH was dispensable. Further experiments are required to fully understand the regulatory roles of the Por1/2 NAH domains.
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