On GxxxG in N-terminal stretches of type-1 VDAC/porin: critical in vertebrate apoptosis, missing in plants

On GxxxG in N-terminal stretches of type-1 VDAC/porin: critical in vertebrate apoptosis, missing... Plant Mol Biol (2012) 79:1–3 DOI 10.1007/s11103-012-9900-7 LETTE R T O T HE EDI T OR On GxxxG in N-terminal stretches of type-1 VDAC/porin: critical in vertebrate apoptosis, missing in plants Friedrich P. Thinnes Received: 14 February 2012 / Accepted: 29 February 2012 / Published online: 27 March 2012 Springer Science+Business Media B.V. 2012 The recently published paper by Teijido et al. 2012 refines Plasmalemmal type-1 VDAC is a candidate for the the voltage-dependent anion channel (VDAC) model pro- VSOAC (Thinnes et al. 1990, 2000; Okada et al. 2004; posed by Marco Colombini (Colombini 2009). It also refers Parsons et al. 2011). Additionally, this VDAC is engaged to data on the accessibility of the VDAC’s N-terminus at in the apoptotic processes that occur in vertebrates, starting the cytosolic side of mitochondria (De Pinto et al. 1991; with apoptotic volume decrease (AVD) (Elinder et al. Guo et al. 1995). The traditional view is in trouble since 2005; Akanda et al. 2008; Thinnes 2009b, c; Thinnes 2011; crystallographic investigations on mammalian type-1 Hur et al. 2012; Marin et al. 2012). For a recent discussion VDAC point to a ß-barrel structure, with the N-terminal of data on cell membrane standing VDAC, the http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Molecular Biology Springer Journals

On GxxxG in N-terminal stretches of type-1 VDAC/porin: critical in vertebrate apoptosis, missing in plants

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Publisher
Springer Netherlands
Copyright
Copyright © 2012 by Springer Science+Business Media B.V.
Subject
Life Sciences; Plant Pathology; Biochemistry, general; Plant Sciences
ISSN
0167-4412
eISSN
1573-5028
D.O.I.
10.1007/s11103-012-9900-7
Publisher site
See Article on Publisher Site

Abstract

Plant Mol Biol (2012) 79:1–3 DOI 10.1007/s11103-012-9900-7 LETTE R T O T HE EDI T OR On GxxxG in N-terminal stretches of type-1 VDAC/porin: critical in vertebrate apoptosis, missing in plants Friedrich P. Thinnes Received: 14 February 2012 / Accepted: 29 February 2012 / Published online: 27 March 2012 Springer Science+Business Media B.V. 2012 The recently published paper by Teijido et al. 2012 refines Plasmalemmal type-1 VDAC is a candidate for the the voltage-dependent anion channel (VDAC) model pro- VSOAC (Thinnes et al. 1990, 2000; Okada et al. 2004; posed by Marco Colombini (Colombini 2009). It also refers Parsons et al. 2011). Additionally, this VDAC is engaged to data on the accessibility of the VDAC’s N-terminus at in the apoptotic processes that occur in vertebrates, starting the cytosolic side of mitochondria (De Pinto et al. 1991; with apoptotic volume decrease (AVD) (Elinder et al. Guo et al. 1995). The traditional view is in trouble since 2005; Akanda et al. 2008; Thinnes 2009b, c; Thinnes 2011; crystallographic investigations on mammalian type-1 Hur et al. 2012; Marin et al. 2012). For a recent discussion VDAC point to a ß-barrel structure, with the N-terminal of data on cell membrane standing VDAC, the

Journal

Plant Molecular Biology – Springer Journals

Published: Mar 27, 2012

References

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    Akanda, N; Tofighi, R; Brask, J; Tamm, C; Elinder, F; Ceccatelli, S
  • The published 3D structure of the VDAC channel: native or not?
    Colombini, M
  • Sequence motifs, polar interactions and conformational changes in helical membrane proteins
    Curran, AR; Engelman, DM
  • Peptide-specific antibodies and proteases as probes of the transmembrane topology of the bovine heart mitochondrial porin
    Pinto, V; Prezioso, G; Thinnes, F; Link, TA; Palmieri, F
  • Opening of plasma membrane voltage-dependent anion channels (VDAC) precedes caspase activation in neuronal apoptosis induced by toxic stimuli
    Elinder, F; Akanda, N; Tofighi, R; Shimizu, S; Tsujimoto, Y; Orrenius, S; Ceccatelli, S
  • Channel active mammalian porin, purified from crude membrane fractions of human B lymphocytes and bovine skeletal muscle, reversibly binds adenosine triphosphate (ATP)
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  • Voltage-dependent-anion-channels (VDAC) in Arabidopsis have a dual localization in the cell but show a distinct role in mitochondria
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  • Human type-1 VDAC, a cisplatin target involved in either apoptotic pathway
    Thinnes, FP
  • Neuroendocrine differentiation of LNCaP cells suggests: VDAC in the cell membrane is involved in the extrinsic apoptotic pathway
    Thinnes, FP
  • Amyloid Aß, cut from APP by ß-secretase BACE1 and γ-secretase, induces apoptosis via opening type-1 porin/VDAC in cell membranes of hypometabolic cells-A basic model for the induction of apoptosis!?
    Thinnes, FP
  • Apoptogenic interactions of plasmalemmal type-1 VDAC and Aβ peptides via GxxxG motifs induce Alzheimer’s disease—a basic model of apoptosis?
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  • Studies on human porin XXII: cell membrane integrated human porin channels are involved in regulatory volume decrease (RVD) of HeLa cells
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  • An N-terminal nucleotide-binding site in VDAC1: involvement in regulating mitochondrial function
    Yehezkel, G; Abu-Hamad, S; Shoshan-Barmatz, V

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