ArticleEukaryotic cell2012
Mitochondrial porin Por1 and its homolog Por2 contribute to the positive control of Snf1 protein kinase in Saccharomyces cerevisiae.
Article in Eukaryotic cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 24 citations in OpenAlex.
- The yeast mitochondrial porin represses Snf1/AMP kinase signaling to attenuate viral replication.Genetics · 2026Article
- The N-terminal α helix domain of the mitochondrial VDAC protein Por2 is dispensable for promoting the nuclear localization of yeast AMPK.microPublication biology · 2026Article
- The small GTPase Rho5-Yet another player in yeast glucose signaling.PLoS genetics · 2025Article
- A dynamic actin cytoskeleton is required to prevent constitutive VDAC-dependent MAPK signalling and aberrant lipid homeostasis.iScience · 2023Article
- The mitospecific domain of Mrp7 (bL27) supports mitochondrial translation during fermentation and is required for effective adaptation to respiration.Molecular biology of the cell · 2022Article
- Porin 1 Modulates Autophagy in Yeast.Cells · 2021Article
- Integrated Multi-Omics Analysis of Mechanisms Underlying Yeast Ethanol Tolerance.Journal of proteome research · 2021Article
- Voltage-Dependent Anion Selective Channel Isoforms in Yeast: Expression, Structure, and Functions.Frontiers in physiology · 2021Review
- Mitochondria-cytosol-nucleus crosstalk: learning from Saccharomyces cerevisiae.FEMS yeast research · 2018Review
- Snf1 cooperates with the CWI MAPK pathway to mediate the degradation of Med13 following oxidative stress.Microbial cell (Graz, Austria) · 2018Article
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Authors and funding
4 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Saccharomyces cerevisiae Snf1 is a member of the conserved Snf1/AMP-activated protein kinase (Snf1/AMPK) family involved in regulating responses to energy limitation, which is detected by mechanisms that include sensing adenine nucleotides. Mitochondrial voltage-dependent anion channel (VDAC) proteins, also known as mitochondrial porins, are conserved in eukaryotes from yeast to humans and play key roles in mediating mitochondrial outer membrane permeability to small metabolites, including ATP, ADP, and AMP. We previously recovered the yeast mitochondrial porin Por1 (yVDAC1) from a two-hybrid screen for Snf1-interacting proteins. Here, we present evidence that Snf1 interacts with Por1 and its homolog Por2 (yVDAC2). Cells lacking Por1 and Por2, but not respiratory-deficient rho(0) cells lacking the mitochondrial genome, exhibit reduced Snf1 activation loop phosphorylation in response to glucose limitation. Thus, Por1 and Por2 contribute to the positive control of Snf1 protein kinase. Physical proximity to the VDAC proteins and mitochondrial surface could facilitate Snf1's ability to sense energy limitation.
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