The Yeast Voltage-Dependent Anion Channel Porin: More IMPORTant than Just Metabolite Transport

Edwards, Ruairidh; Tokatlidis, Kostas

doi:10.1016/j.molcel.2019.02.028

Cited by 3 publications

(3 citation statements)

References 9 publications

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“…In this contest, yVDAC1 was individuated as a coupling factor for protein translocation of carrier precursors into the inner mitochondrial membrane (IMM) (Ellenrieder et al, 2019). Notably, both these works supported this brand new role of yVDAC1 independent of its metabolic function (Edwards and Tokatlidis, 2019).…”

Section: Yeast Vdac1 Is Essential For the Proper Maintenance Of Mitochondriamentioning

confidence: 84%

Voltage-Dependent Anion Selective Channel Isoforms in Yeast: Expression, Structure, and Functions

et al. 2021

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Mitochondrial porins, also known as voltage-dependent anion selective channels (VDACs), are pore-forming molecules of the outer mitochondrial membranes, involved in the regulation of metabolic flux between cytosol and mitochondria. Playing such an essential role, VDAC proteins are evolutionary conserved and isoforms are present in numerous species. The quest for specific function(s) related to the raise of multiple isoforms is an intriguing theme. The yeast Saccharomyces cerevisiae genome is endowed with two different VDAC genes encoding for two distinct porin isoforms, definitely less characterized in comparison to mammalian counterpart. While yVDAC1 has been extensively studied, the second isoform, yVDAC2, is much less expressed, and has a still misunderstood function. This review will recapitulate the known and poorly known information in the literature, in the light of the growing interest about the features of VDAC isoforms in the cell.

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Section: Yeast Vdac1 Is Essential For the Proper Maintenance Of Mitochondriamentioning

confidence: 84%

Voltage-Dependent Anion Selective Channel Isoforms in Yeast: Expression, Structure, and Functions

et al. 2021

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“…Combined, this highlights a divergent translocation mechanism for Mia40 substrates compared to matrix and inner membrane targeted proteins that are imported through the TOM complex in a different manner. Furthermore, substrates of Mia40 are thought to engage for import via a small population of dimeric TOM complexes [40][41][42][43]. This differs from all the other import pathways which engage via the more abundant trimeric TOM complex.…”

Section: Mia40 Substrate Translocation and Recognitionmentioning

confidence: 99%

The mitochondrial intermembrane space: the most constricted mitochondrial sub-compartment with the largest variety of protein import pathways

2021

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The mitochondrial intermembrane space (IMS) is the most constricted sub-mitochondrial compartment, housing only about 5% of the mitochondrial proteome, and yet is endowed with the largest variability of protein import mechanisms. In this review, we summarize our current knowledge of the major IMS import pathway based on the oxidative protein folding pathway and discuss the stunning variability of other IMS protein import pathways. As IMS-localized proteins only have to cross the outer mitochondrial membrane, they do not require energy sources like ATP hydrolysis in the mitochondrial matrix or the inner membrane electrochemical potential which are critical for import into the matrix or insertion into the inner membrane. We also explore several atypical IMS import pathways that are still not very well understood and are guided by poorly defined or completely unknown targeting peptides. Importantly, many of the IMS proteins are linked to several human diseases, and it is therefore crucial to understand how they reach their normal site of function in the IMS. In the final part of this review, we discuss current understanding of how such IMS protein underpin a large spectrum of human disorders.

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“…Interestingly, the outer membrane metabolite channel porin was recently identified to have a role in carrier protein biogenesis and bound directly to carrier protein precursors as well as directly recruiting TIM22 (Ellenrieder et al, 2019). The exact mechanism by which porin aids carrier insertion remains unknown but may involve physically linking the inner and outer membranes through these protein-protein interactions given that a direct TOM-TIM22 supercomplex does not appear to exist (Edwards and Tokatlidis, 2019;Ellenrieder et al, 2019;Horten et al, 2020).…”

Section: Figure 5 |mentioning

confidence: 99%

Targeting and Insertion of Membrane Proteins in Mitochondria

Eaglesfield

Tokatlidis

2021

Front. Cell Dev. Biol.

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Mitochondrial membrane proteins play an essential role in all major mitochondrial functions. The respiratory complexes of the inner membrane are key for the generation of energy. The carrier proteins for the influx/efflux of essential metabolites to/from the matrix. Many other inner membrane proteins play critical roles in the import and processing of nuclear encoded proteins (∼99% of all mitochondrial proteins). The outer membrane provides another lipidic barrier to nuclear-encoded protein translocation and is home to many proteins involved in the import process, maintenance of ionic balance, as well as the assembly of outer membrane components. While many aspects of the import and assembly pathways of mitochondrial membrane proteins have been elucidated, many open questions remain, especially surrounding the assembly of the respiratory complexes where certain highly hydrophobic subunits are encoded by the mitochondrial DNA and synthesised and inserted into the membrane from the matrix side. This review will examine the various assembly pathways for inner and outer mitochondrial membrane proteins while discussing the most recent structural and biochemical data examining the biogenesis process.

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The Yeast Voltage-Dependent Anion Channel Porin: More IMPORTant than Just Metabolite Transport

Cited by 3 publications

References 9 publications

Voltage-Dependent Anion Selective Channel Isoforms in Yeast: Expression, Structure, and Functions

Voltage-Dependent Anion Selective Channel Isoforms in Yeast: Expression, Structure, and Functions

The mitochondrial intermembrane space: the most constricted mitochondrial sub-compartment with the largest variety of protein import pathways

Targeting and Insertion of Membrane Proteins in Mitochondria

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