Voltage-dependent-anion-channels (VDACs) in Arabidopsis have a dual localization in the cell but show a distinct role in mitochondria

Robert, Nadia; d’Erfurth, Isabelle; Marmagne, Anne; Erhardt, Mathieu; Allot, Michèle; Boivin, K.; Gissot, Lionel; Monachello, Dario; Michaud, Morgane; Duchêne, Anne‐Marie; Barbier‐Brygoo, Hélène; Maréchal-Drouard, Laurence; Ephritikhine, Geneviève; Filleur, Sophie

doi:10.1007/s11103-012-9874-5

Cited by 55 publications

(64 citation statements)

References 78 publications

(103 reference statements)

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“…Moreover, they are found in various membranes-in particular, in nonmitochondrial ones (18,19). Four nucleus-encoded VDACs (VDAC1-4) have been identified in At, and the specific function of each isoform is still poorly understood (20,21). In this study, we show that APA produces two major isoforms of VDAC3 transcripts (At5g15090) that differ by the length of their 3′ UTR, one being 140 nt longer than the other.…”

mentioning

confidence: 72%

“…Four VDAC genes are ubiquitously expressed in At, even if their expression patterns present clear differences (Genevestigator) (20,21). Apart from their conserved role in metabolite exchanges, the specific role of each VDAC is still unknown.…”

Section: Discussionmentioning

confidence: 99%

“…Apart from their conserved role in metabolite exchanges, the specific role of each VDAC is still unknown. The four proteins are found in mitochondria, and three of the four are also detected in the plasma membrane (21). KO mutants for VDAC1, VDAC2, and VDAC4 present growth-delay phenotypes, distorted leaves and reduce fertility.…”

Section: Discussionmentioning

confidence: 99%

“…So the simplest hypothesis for VDAC3 mRNA targeting is that it allows a more efficient import of VDAC3 protein into mitochondria. The vdac3 mutants have no phenotype under normal growth conditions (20)(21)(22), so they cannot be used for complementation analyses. Because VDAC1 is the closest VDAC3 paralog (18), we transformed a vdac1 T-DNA insertion line (SALK_034653) with two VDAC3 transgenes harboring a HA tag at the N terminus of CDS and differing by their 3′ extensions (cUTR or aUTR sequences; Fig.…”

Section: Vdac3-cutr and Vdac3-autr Differentially Impact The Mitochonmentioning

confidence: 99%

“…S3 A and B). Vdac1 mutant shows phenotypes associated with mitochondrial dysfunctions, with distorted rosette and cauline leaves, delayed development, and reduced fertility (21) (Fig. 5A).…”

Section: Vdac3-cutr and Vdac3-autr Differentially Impact The Mitochonmentioning

confidence: 99%

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Differential targeting of VDAC3 mRNA isoforms influences mitochondria morphology

Michaud

Ubrig

Filleur

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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Intracellular targeting of mRNAs has recently emerged as a prevalent mechanism to control protein localization. For mitochondria, a cotranslational model of protein import is now proposed in parallel to the conventional posttranslational model, and mitochondrial targeting of mRNAs has been demonstrated in various organisms. Voltage-dependent anion channels (VDACs) are the most abundant proteins in the outer mitochondrial membrane and the major transport pathway for numerous metabolites. Four nucleus-encoded VDACs have been identified in Arabidopsis thaliana. Alternative cleavage and polyadenylation generate two VDAC3 mRNA isoforms differing by their 3′ UTR. By using quantitative RT-PCR and in vivo mRNA visualization approaches, the two mRNA variants were shown differentially associated with mitochondria. The longest mRNA presents a 3′ extension named alternative UTR (aUTR) that is necessary and sufficient to target VDAC3 mRNA to the mitochondrial surface. Moreover, aUTR is sufficient for the mitochondrial targeting of a reporter transcript, and can be used as a tool to target an unrelated mRNA to the mitochondrial surface. Finally, VDAC3-aUTR mRNA variant impacts mitochondria morphology and size, demonstrating the role of mRNA targeting in mitochondria biogenesis.mRNA localization | mRNA sorting | green RNA | porin | plant E ukaryotic cells are characterized by compartmentalization of functions in complex organelles, and cell activity depends on synthesis and precise localization of proteins. The mechanisms of protein sorting are the subject of intense research, and models are often reevaluated (1). The earliest models for protein localization were based on the presence of targeting signals in the polypeptide sequences. However, the targeting of mRNAs to various subcellular regions has recently emerged as an essential regulatory step for protein localization (2).Mitochondria contain hundreds of proteins, but only a few are encoded by the mitochondrial genome. The other proteins are nucleus-encoded and imported into the organelle. Protein import into mitochondria is controlled by peptide sequences that are recognized by mitochondrial receptors (3, 4). In parallel with this posttranslational model, a cotranslational model is now emerging (2, 5). A microarray analysis in Saccharomyces cerevisiae has shown that approximately half of the mRNAs encoding mitochondrial proteins are found in the vicinity of mitochondria (6). Mitochondrial targeting of mRNA was also demonstrated in mammals and plants (7,8).Mechanisms of mitochondrial targeting of mRNAs were essentially studied in yeast. In this species, three factors have been clearly identified to influence mRNA targeting to the mitochondrial surface. (i) Targeting of many but not all mRNAs appears dependent on translation (9, 10). (ii) The RNA-binding protein Puf3p is essential for mitochondrial targeting of a subset of mRNAs (9). (iii) The translocase of the outer mitochondrial membrane (TOM complex) is also involved in mRNA binding (10-12). In addition, some mRNAs are...

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mentioning

confidence: 72%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Vdac3-cutr and Vdac3-autr Differentially Impact The Mitochonmentioning

confidence: 99%

Section: Vdac3-cutr and Vdac3-autr Differentially Impact The Mitochonmentioning

confidence: 99%

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Differential targeting of VDAC3 mRNA isoforms influences mitochondria morphology

Michaud

Ubrig

Filleur

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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Plant VDAC Permeability: Molecular Basis and Role in Oxidative Stress

Homblé¹,

Kmita²,

Saidani³

et al. 2017

Molecular Basis for Mitochondrial Signaling

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The mitochondrial voltage-dependent anion-selective channel (VDAC) is highly abundant in the mitochondrial outer membrane. It is permeable to molecules with a size up to about 5kDa and is the main pathway for the exchange of metabolites and ions between the mitochondrial intermembrane space and the cytosol. Experimental studies performed for plant VDAC have shown that the channel displays properties reported for VDACs of other eukaryotic organisms. Firstly, it transports compounds as diverse as inorganic ions (e.g., K + and Cl -), adenylates (e.g., ATP and AMP) and large macromolecules (tRNA and DNA). Secondly, despite its wide pore, the channel displays selectivity towards these compounds, i.e. it distinguishes between K + and Clbut also between ATP and AMP. The question of how VDAC can selectively transport these different compounds is addressed in this chapter based on data obtained for plant VDAC. It is well known that all organisms have at least one canonical VDAC isoform that shares similar electrophysiological properties and secondary structure with cognate VDAC of other organisms. For instance, this is the case of the mammalian VDAC1, the yeast Saccharomyces cerevisiae VDAC1 and the PcVDAC purified from the bean Phaseolus coccineus seeds. Consequently, Brownian dynamic simulations of monatomic ion permeation through the experimental threedimensional structure of the mammalian VDAC1 and the PcVDAC modeled structure predict fairly well conductance and selectivity of both the proteins. In addition, the data of molecular simulation studies performed on the mammalian VDAC1 agree with the experimental data obtained for PcVDAC, which suggests a similar permeation process for these VDAC proteins. Accordingly, both the experimental and theoretical studies indicate that the selectivity for inorganic ions is a consequence of the excess of positive charges and their distribution inside the pore and the absence of defined pathways for the permeation. In contrast, the permeation of metabolites involves a major binding site located at the N-terminal helix which folded into the pore lumen and occurs through a preferential pathway. The key residues forming the binding site are conserved in the PcVDAC pointing to the conserved permeation process. The process might be affected by VDAC-interaction with other proteins. For example, it is suggested that plant VDAC is involved in the oxidative stress response which includes cytosolic hexokinase and thioredoxin binding to VDAC. This in turn may influence the exchange of molecules between mitochondria and the cytosol.

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Plant mitochondrial FMT and its mammalian homolog CLUH controls development and behavior in Arabidopsis and locomotion in mice

Ralevski

Apelt

Olas

et al. 2022

Cell. Mol. Life Sci.

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Voltage-dependent-anion-channels (VDACs) in Arabidopsis have a dual localization in the cell but show a distinct role in mitochondria

Cited by 55 publications

References 78 publications

Differential targeting of VDAC3 mRNA isoforms influences mitochondria morphology

Differential targeting of VDAC3 mRNA isoforms influences mitochondria morphology

Plant VDAC Permeability: Molecular Basis and Role in Oxidative Stress

Plant mitochondrial FMT and its mammalian homolog CLUH controls development and behavior in Arabidopsis and locomotion in mice

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