Voltage-dependent anion channels: the wizard of the mitochondrial outer membrane

Mertins, Barbara; Psakis, Georgios; Essen, Lars‐Oliver

doi:10.1515/hsz-2014-0203

Cited by 40 publications

(32 citation statements)

References 43 publications

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“…Two cysteine residues in the N-terminus (C2, C8) are able to cause pore restriction through disulphide bond formation with C122, leading the authors to present a model in which these bonds trap the N-terminus in the barrel, generating an ungated, low conductance pore depending on the redox state [31], implying that the conductance of hVDAC3 is responsive to redox state [33]. [62]. Based on the structure of mVDAC1 [20], C122 is located in the turn between ß7 and ß8, and K119 is at the C-terminal end of ß7.…”

Section: Accepted Manuscriptmentioning

confidence: 99%

“…Panels C and D highlight residues that were specifically targeted in recent studies of gating. The effects of crosslinking L10C and A170C were tested in [60]; T6C was crosslinked to K197 and K224 [54], and the pairs of V3C / K119C and A14C / S193C were involved in cross-linking experiments [62], and variants with replacements of R15P/D16P or G21A/G23A in rVDAC1 were utilized in gating experiments [54] and are modeled on the very similar human and mouse sequences. Images were created with MacPyMOL [85].…”

Section: Accepted Manuscriptmentioning

confidence: 99%

“…Gating occurs at +/-50 mV, when the interactions between the Nterminus and the barrel that stabilize the open state are disrupted. B) Normal gating in the crosslinked V3C/K119C variant[62]. The cross-link between the tip of the N-terminus and ß7 does not disrupt the movement of the N-terminus in a way that prevents normal gating.…”

mentioning

confidence: 99%

“…The cross-link between the tip of the N-terminus and ß7 does not disrupt the movement of the N-terminus in a way that prevents normal gating. C)Crosslinking of A14C to S193C in ß13[62] traps the central part of the N-terminus against the barrel wall, preventing its release and trapping the barrel in an open conformation. D) Gating of crosslinked variant L10C/A170C.…”

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confidence: 99%

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The N-terminus of VDAC: Structure, mutational analysis, and a potential role in regulating barrel shape

Shuvo

Ferens

Court

2016

Biochimica et Biophysica Acta (BBA) - Biomembranes

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A novel feature of the voltage-dependent anion channel (VDAC, mitochondrial porin), is the barrel, comprising an odd number of β-strands and closed by parallel strands. Recent research has focused on the N-terminal segment, which in the available structures, resides in the lumen and is not part of the barrel. In this review, the structural data obtained from vertebrate VDAC are integrated with those from VDAC in artificial bilayers, emphasizing the array of native and tagged versions of VDAC used. The data are discussed with respect to a recent gating model (Zachariae et al. (2012) Structure 20:1-10), in which the N-terminus acts not as a gate on a stable barrel, but rather stabilizes the barrel, preventing its shift into a partially collapsed, low-conductance, closed state. Additionally, the role of the N-terminus in VDAC oligomerization, apoptosis through interactions with hexokinase and its interaction with ATP are discussed briefly.

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Section: Accepted Manuscriptmentioning

confidence: 99%

Section: Accepted Manuscriptmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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The N-terminus of VDAC: Structure, mutational analysis, and a potential role in regulating barrel shape

Shuvo

Ferens

Court

2016

Biochimica et Biophysica Acta (BBA) - Biomembranes

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“…This pattern of shifting pI with time is likely a result of PTMs that alter protein charge while minimally impacting M r . VDAC2 is an important component of the mitochondrial outer membrane permeability pore, which allows movement of ions and metabolites between the cytosol and the intermembrane space (Mertins et al, 2014). [Note that despite the nomenclature, it appears that bivalves have only one VDAC isoform, whereas mammals have three (Shoshan-Barmatz et al, 2010).]…”

Section: Discussionmentioning

confidence: 99%

Rapid proteomic responses to a near-lethal heat stress in the salt marsh musselGeukensia demissa

Fields

Burmester

Cox

et al. 2016

Journal of Experimental Biology

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Acute heat stress perturbs cellular function on a variety of levels, leading to protein dysfunction and aggregation, oxidative stress and loss of metabolic homeostasis. If these challenges are not overcome quickly, the stressed organism can die. To better understand the earliest tissue-level responses to heat stress, we examined the proteomic response of gill from Geukensia demissa, an extremely eurythermal mussel from the temperate intertidal zone of eastern North America. We exposed 15°C-acclimated individuals to an acute near-lethal heat stress (45°C) for 1 h, and collected gill samples from 0 to 24 h of recovery. The changes in protein expression we found reveal a coordinated physiological response to acute heat stress: proteins associated with apoptotic processes were increased in abundance during the stress itself (i.e. at 0 h of recovery), while protein chaperones and foldases increased in abundance soon after (3 h). The greatest number of proteins changed abundance at 6 h; these included oxidative stress proteins and enzymes of energy metabolism. Proteins associated with the cytoskeleton and extracellular matrix also changed in abundance starting at 6 h, providing evidence of cell proliferation, migration and tissue remodeling. By 12 h, the response to acute heat stress was diminishing, with fewer stress and structural proteins changing in abundance. Finally, the proteins with altered abundances identified at 24 h suggest a return to the pre-stress anabolic state.

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Mitochondrial Outer Membrane Channels: Emerging Diversity in Transport Processes

Becker

Wagner

2018

BioEssays

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Mitochondrial function and biogenesis depend on the transport of a large variety of proteins, ions, and metabolites across the two surrounding membranes. While several specific transporters are present in the inner membrane, transport processes across the outer membrane are less understood. Recent studies reveal that the number of outer membrane channels and their transport mechanisms are more diverse than originally thought. Four protein-conducting channels promote transport of distinct sets of precursor proteins across and into the outer membrane. The voltage-dependent anion channel (VDAC) forms the major channel for small hydrophilic molecules. In addition, three channels with yet unknown substrate specificity exist in the outer membrane. In this review, we outline the emerging functional diversity, selectivity, and regulation of mitochondrial outer membrane channels. The presence of several channel-forming proteins challenges the traditional view that the outer membrane forms an unspecific size-exclusion filter for the flux of small hydrophilic molecules.

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Voltage-dependent anion channels: the wizard of the mitochondrial outer membrane

Cited by 40 publications

References 43 publications

The N-terminus of VDAC: Structure, mutational analysis, and a potential role in regulating barrel shape

The N-terminus of VDAC: Structure, mutational analysis, and a potential role in regulating barrel shape

Rapid proteomic responses to a near-lethal heat stress in the salt marsh musselGeukensia demissa

Mitochondrial Outer Membrane Channels: Emerging Diversity in Transport Processes

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