Literature DB >> 2461874

The mitochondrial outer membrane channel, VDAC, is modulated by a soluble protein.

M J Holden1, M Colombini.   

Abstract

The mitochondrial outer membrane channel, VDAC, serves as the primary permeability pathway for metabolite flux between cytoplasmic and mitochondrial compartments. VDAC can occupy several conformational states differing in ion conductivity. Small transmembrane potentials cause transitions from open- to closed-channel conformations. A soluble mitochondrial protein enhances the channel's response to voltage by increasing the rate of channel closing; inducing the occupation of lower conductance states; and decreasing the rate of channel reopening. This protein modulator acts at very low concentrations and its role in the cell may be to regulate the permeability of the mitochondrial outer membrane by inducing channel closure.

Mesh:

Substances:

Year:  1988        PMID: 2461874     DOI: 10.1016/0014-5793(88)81040-8

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  36 in total

Review 1.  Ion channels in the outer membranes of chloroplasts and mitochondria: open doors or regulated gates?

Authors:  B Bölter; J Soll
Journal:  EMBO J       Date:  2001-03-01       Impact factor: 11.598

2.  The role of sterols in the functional reconstitution of water-soluble mitochondrial porins from plants.

Authors:  F Carbonara; B Popp; A Schmid; V Iacobazzi; G Genchi; F Palmieri; R Benz
Journal:  J Bioenerg Biomembr       Date:  1996-04       Impact factor: 2.945

3.  A soluble mitochondrial protein increases the voltage dependence of the mitochondrial channel, VDAC.

Authors:  M Y Liu; M Colombini
Journal:  J Bioenerg Biomembr       Date:  1992-02       Impact factor: 2.945

Review 4.  Toward the molecular structure of the mitochondrial channel, VDAC.

Authors:  C A Mannella; M Forte; M Colombini
Journal:  J Bioenerg Biomembr       Date:  1992-02       Impact factor: 2.945

Review 5.  Evidence for extra-mitochondrial localization of the VDAC/porin channel in eucaryotic cells.

Authors:  F P Thinnes
Journal:  J Bioenerg Biomembr       Date:  1992-02       Impact factor: 2.945

6.  Classification of projection images of crystalline arrays of the mitochondrial, voltage-dependent anion-selective channel embedded in aurothioglucose.

Authors:  X W Guo; C A Mannella
Journal:  Biophys J       Date:  1992-08       Impact factor: 4.033

7.  Binding of a synthetic targeting peptide to a mitochondrial channel protein.

Authors:  C A Mannella; X W Guo; J Dias
Journal:  J Bioenerg Biomembr       Date:  1992-02       Impact factor: 2.945

8.  VDAC: the channel at the interface between mitochondria and the cytosol.

Authors:  Marco Colombini
Journal:  Mol Cell Biochem       Date:  2004 Jan-Feb       Impact factor: 3.396

Review 9.  The voltage-dependent anion channel in endoplasmic/sarcoplasmic reticulum: characterization, modulation and possible function.

Authors:  V Shoshan-Barmatz; A Israelson
Journal:  J Membr Biol       Date:  2005-03       Impact factor: 1.843

10.  On the role of VDAC in apoptosis: fact and fiction.

Authors:  Tatiana K Rostovtseva; Wenzhi Tan; Marco Colombini
Journal:  J Bioenerg Biomembr       Date:  2005-06       Impact factor: 2.945

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.