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We are analyzing https://link.springer.com/article/10.1007/s002329900540.

Title:
Mouse VDAC Isoforms Expressed in Yeast: Channel Properties and Their Roles in Mitochondrial Outer Membrane Permeability | The Journal of Membrane Biology
Description:
The channel-forming protein called VDAC forms the major pathway in the mitochondrial outer membrane and controls metabolite flux across that membrane. The different VDAC isoforms of a species may play different roles in the regulation of mitochondrial functions. The mouse has three VDAC isoforms (VDAC1, VDAC2 and VDAC3). These proteins and different versions of VDAC3 were expressed in yeast cells (S. cerevisiae) missing the major yeast VDAC gene and studied using different approaches. When reconstituted into liposomes, each isoform induced a permeability in the liposomes with a similar molecular weight cutoff (between 3,400 and 6,800 daltons based on permeability to polyethylene glycol). In contrast, electrophysiological studies on purified proteins showed very different channel properties. VDAC1 is the prototypic version whose properties are highly conserved among other species. VDAC2 also has normal gating activity but may exist in 2 forms, one with a lower conductance and selectivity. VDAC3 can also form channels in planar phospholipid membranes. It does not insert readily into membranes and generally does not gate well even at high membrane potentials (up to 80 mV). Isolated mitochondria exhibit large differences in their outer membrane permeability to NADH depending on which of the mouse VDAC proteins was expressed. These differences in permeability could not simply be attributed to different amounts of each protein present in the isolated mitochondria. The roles of these different VDAC proteins are discussed.
Website Age:
28 years and 1 months (reg. 1997-05-29).

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  • Science
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Custom-built

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🌠 Phenomenal Traffic: 5M - 10M visitors per month


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Keywords {πŸ”}

vdac, membrane, article, permeability, proteins, mitochondrial, privacy, cookies, content, journal, outer, information, publish, search, mouse, isoforms, expressed, yeast, properties, roles, channels, access, chapter, data, log, research, biology, channel, decker, sampson, liposomes, molecular, discover, usa, springer, function, optional, personal, parties, policy, find, track, cite, craigen, colombini, explore, protein, forms, major, species,

Topics {βœ’οΈ}

mouse vdac proteins month download article/chapter mitochondrial outer membrane form channels purified proteins showed privacy choices/manage cookies vdac proteins membrane biology aims outer membrane permeability high membrane potentials normal gating activity full article pdf plant vdac permeability european economic area scope submit manuscript controls metabolite flux conditions privacy policy accepting optional cookies planar phospholipid membranes related subjects proteins main content log mitochondrial functions vdac isoforms isolated mitochondria journal finder publish membrane biol check access instant access nadh depending protein present privacy policy personal data similar content vdac structures colombini department books a information article log optional cookies manage preferences major pathway channel properties data protection article cite essential cookies cookies skip subscription content membrane institution subscribe

Schema {πŸ—ΊοΈ}

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         headline:Mouse VDAC Isoforms Expressed in Yeast: Channel Properties and Their Roles in Mitochondrial Outer Membrane Permeability
         description: The channel-forming protein called VDAC forms the major pathway in the mitochondrial outer membrane and controls metabolite flux across that membrane. The different VDAC isoforms of a species may play different roles in the regulation of mitochondrial functions. The mouse has three VDAC isoforms (VDAC1, VDAC2 and VDAC3). These proteins and different versions of VDAC3 were expressed in yeast cells (S. cerevisiae) missing the major yeast VDAC gene and studied using different approaches. When reconstituted into liposomes, each isoform induced a permeability in the liposomes with a similar molecular weight cutoff (between 3,400 and 6,800 daltons based on permeability to polyethylene glycol). In contrast, electrophysiological studies on purified proteins showed very different channel properties. VDAC1 is the prototypic version whose properties are highly conserved among other species. VDAC2 also has normal gating activity but may exist in 2 forms, one with a lower conductance and selectivity. VDAC3 can also form channels in planar phospholipid membranes. It does not insert readily into membranes and generally does not gate well even at high membrane potentials (up to 80 mV). Isolated mitochondria exhibit large differences in their outer membrane permeability to NADH depending on which of the mouse VDAC proteins was expressed. These differences in permeability could not simply be attributed to different amounts of each protein present in the isolated mitochondria. The roles of these different VDAC proteins are discussed.
         datePublished:
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         pageStart:89
         pageEnd:102
         sameAs:https://doi.org/10.1007/s002329900540
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            Key words: Electrophysiology β€” Insertion β€” Gating β€” NADH β€” Liposomes
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            Human Physiology
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      headline:Mouse VDAC Isoforms Expressed in Yeast: Channel Properties and Their Roles in Mitochondrial Outer Membrane Permeability
      description: The channel-forming protein called VDAC forms the major pathway in the mitochondrial outer membrane and controls metabolite flux across that membrane. The different VDAC isoforms of a species may play different roles in the regulation of mitochondrial functions. The mouse has three VDAC isoforms (VDAC1, VDAC2 and VDAC3). These proteins and different versions of VDAC3 were expressed in yeast cells (S. cerevisiae) missing the major yeast VDAC gene and studied using different approaches. When reconstituted into liposomes, each isoform induced a permeability in the liposomes with a similar molecular weight cutoff (between 3,400 and 6,800 daltons based on permeability to polyethylene glycol). In contrast, electrophysiological studies on purified proteins showed very different channel properties. VDAC1 is the prototypic version whose properties are highly conserved among other species. VDAC2 also has normal gating activity but may exist in 2 forms, one with a lower conductance and selectivity. VDAC3 can also form channels in planar phospholipid membranes. It does not insert readily into membranes and generally does not gate well even at high membrane potentials (up to 80 mV). Isolated mitochondria exhibit large differences in their outer membrane permeability to NADH depending on which of the mouse VDAC proteins was expressed. These differences in permeability could not simply be attributed to different amounts of each protein present in the isolated mitochondria. The roles of these different VDAC proteins are discussed.
      datePublished:
      dateModified:
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         Key words: Electrophysiology β€” Insertion β€” Gating β€” NADH β€” Liposomes
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         Human Physiology
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