title: New functions of an old protein: the eukaryotic porin or voltage dependent anion selective channel (VDAC).
abstract: Mitochondrial porin or VDAC (Voltage Dependent Anion selective Channels) was identified for the first time in 1976, on the basis of the evolutionary similarity between the gram negative and mitochondrial outer membranes. Since this achievement VDAC has been extensively investigated: its functional features have been sharply defined upon reconstitution in artificial membranes and its sequence has been determined in many genomes. Unfortunately the tertiary structure has not yet been solved, mainly because it proved to be very difficult to get suitable crystals. Despite this established knowledge, in the last few years this protein has attracted renewed interest. There are two main reasons for this interest: the discovery, in most eukaryotes, of a family of genes encoding VDAC isoforms and the claims of VDAC involvement in the intrinsic pathway of apoptosis and in particular in the mechanism of cytochrome c release from mitochondria. We can affirm that nowadays the eukaryotic porin (or VDAC) is studied in a more general cellular contest, looking at the interactions and integration with other molecules, since VDAC is in a crucial position in the cell, forming the main interface between the mitochondrial and the cellular metabolisms. In this minireview we will briefly focus our attention onto the following topics: 1) recent advances about the structure of VDAC; 2) the VDAC-related multigene families; 3) the presence, targeting and function of VDAC in various cell membranes.
authors.affiliation: Lab. of Biochemistry and Molecular Biology, Dept. of Chemical Sciences, University of Catania, Catania, Italy. vdpbiofa@mbox.unict.it
authors.forename: Vito
authors.initials: V
authors.lastname: De Pinto
authors.forename: Angela
authors.initials: A
authors.lastname: Messina
authors.forename: Rosita
authors.initials: R
authors.lastname: Accardi
authors.forename: Rita
authors.initials: R
authors.lastname: Aiello
authors.forename: Francesca
authors.initials: F
authors.lastname: Guarino
authors.forename: Marianna Flora
authors.initials: MF
authors.lastname: Tomasello
authors.forename: Massimo
authors.initials: M
authors.lastname: Tommasino
authors.forename: Gianluca
authors.initials: G
authors.lastname: Tasco
authors.forename: Rita
authors.initials: R
authors.lastname: Casadio
authors.forename: Roland
authors.initials: R
authors.lastname: Benz
authors.forename: Francesca
authors.initials: F
authors.lastname: De Giorgi
authors.forename: François
authors.initials: F
authors.lastname: Ichas
authors.forename: Mark
authors.initials: M
authors.lastname: Baker
authors.forename: Alfons
authors.initials: A
authors.lastname: Lawen
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D006801:Humans; D008928:Mitochondria / Q000378:metabolism; D008957:Models, Genetic; D008958:Models, Molecular; D005810:Multigene Family; D018272:Porins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D011487:Protein Conformation; D020033:Protein Isoforms; D050996:Voltage-Dependent Anion Channel 2; D050994:Voltage-Dependent Anion Channels
chemical_list: D018272:Porins; D020033:Protein Isoforms; C494765:VDAC2 protein, human; D050996:Voltage-Dependent Anion Channel 2; D050994:Voltage-Dependent Anion Channels