Isolation of a novel human voltage-dependent anion channel gene

Rahmani, Zohra; Maunoury, Catherine; Siddiqui, Aleem

doi:10.1038/sj.ejhg.5200198

Cited by 47 publications

(45 citation statements)

References 20 publications

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“…Another mechanism involving mRNA untranslated regions has also been considered [162]. Three isoforms of mitochondrial porin, VDAC1, VDAC2 and VDAC3, have been cloned in mammals [49,[163][164][165][166][167][168][169][170]. If the maxi-anion channel is a pl-VDAC, then deletion and/or silencing of the VDAC genes would be expected to eliminate the channel activity.…”

Section: Puzzle Of the Molecular Identity Of The Maxi-anion Channelmentioning

confidence: 99%

The maxi-anion channel: a classical channel playing novel roles through an unidentified molecular entity

Sabirov

Okada

2008

J Physiol Sci

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The maxi-anion channel is widely expressed and found in almost every part of the body. The channel is activated in response to osmotic cell swelling, to excision of the membrane patch, and also to some other physiologically and pathophysiologically relevant stimuli, such as salt stress in kidney macula densa as well as ischemia/ hypoxia in heart and brain. Biophysically, the maxi-anion channel is characterized by a large single-channel conductance of 300-400 pS, which saturates at 580-640 pS with increasing the Cl -concentration. The channel discriminates well between Na ? and Cl -, but is poorly selective to other halides exhibiting weak electric-field selectivity with an Eisenman's selectivity sequence I. The maxi-anion channel has a wide pore with an effective radius of *1.3 nm and permits passage not only of Cl -but also of some intracellular large organic anions, thereby releasing major extracellular signals and gliotransmitters such as glutamate -and ATP 4-. The channel-mediated efflux of these signaling molecules is associated with kidney tubuloglomerular feedback, cardiac ischemia/hypoxia, as well as brain ischemia/hypoxia and excitotoxic neurodegeneration. Despite the ubiquitous expression, well-defined properties and physiological/pathophysiological significance of this classical channel, the molecular entity has not been identified. Molecular identification of the maxi-anion channel is an urgent task that would greatly promote investigation in the fields not only of anion channel but also of physiological/pathophysiological signaling in the brain, heart and kidney.

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Section: Puzzle Of the Molecular Identity Of The Maxi-anion Channelmentioning

confidence: 99%

The maxi-anion channel: a classical channel playing novel roles through an unidentified molecular entity

Sabirov

Okada

2008

J Physiol Sci

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“…VDAC3 belongs to the mitochondrial porins, but while it shares 60-70% sequence identity with VDAC1 and VDAC2, which regulate mitochondrial energetics, 17,18 the mitochondrial function of VDAC3 is not clear. Moreover, VDAC3 has been found at the non-membranous sperm outer dense fiber, where the maternal centriole protein ODF2 was first identified.…”

Section: Introductionmentioning

confidence: 99%

VDAC3 regulates centriole assembly by targeting Mps1 to centrosomes

et al. 2012

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“…VDAC is a monomeric, voltage-gated channel that allows passage of molecules up to 5,000 daltons (1), and multiple isoforms have been identified in numerous eukaryotic species (2)(3)(4)(5). VDAC provides the predominant pathway for small metabolites such as ATP, ADP, phosphocreatine and small ions across the mitochondrial outer membrane (1,6).…”

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confidence: 99%

Neurologic Dysfunction and Male Infertility in Drosophila porin Mutants

Graham¹,

Li²,

Alesii³

et al. 2010

Journal of Biological Chemistry

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Voltage-dependent anion channels (VDACs) are a family of small pore-forming proteins of the mitochondrial outer membrane found in all eukaryotes. VDACs play an important role in the regulated flux of metabolites between the cytosolic and mitochondrial compartments, and three distinct mammalian isoforms have been identified. Animal and cell culture experiments suggest that the various isoforms act in disparate roles such as apoptosis, synaptic plasticity, learning, muscle bioenergetics, and reproduction. In Drosophila melanogaster, porin is the ubiquitously expressed VDAC isoform. Through imprecise excision of a P element insertion in the porin locus, a series of hypomorphic alleles have been isolated, and analyses of flies homozygous for these mutant alleles reveal phenotypes remarkably reminiscent of mouse VDAC mutants. These include partial lethality, defects of mitochondrial respiration, abnormal muscle mitochondrial morphology, synaptic dysfunction, and male infertility, which are features often observed in human mitochondrial disorders. Furthermore, the observed synaptic dysfunction at the neuromuscular junction in porin mutants is associated with a paucity of mitochondria in presynaptic termini. The similarity of VDAC mutant phenotypes in the fly and mouse clearly indicate a fundamental conservation of VDAC function. The establishment and validation of a new in vivo model for VDAC function in Drosophila should provide a valuable tool for further genetic dissection of VDAC role(s) in mitochondrial biology and disease, and as a model of mitochondrial disorders potentially amenable to the development of treatment strategies.

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Isolation of a novel human voltage-dependent anion channel gene

Cited by 47 publications

References 20 publications

The maxi-anion channel: a classical channel playing novel roles through an unidentified molecular entity

The maxi-anion channel: a classical channel playing novel roles through an unidentified molecular entity

VDAC3 regulates centriole assembly by targeting Mps1 to centrosomes

Neurologic Dysfunction and Male Infertility in Drosophila porin Mutants

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