TY - JOUR
T1 - ANT-VDAC1 interaction is direct and depends on ANT isoform conformation in vitro
AU - Allouche, Maya
AU - Pertuiset, Claire
AU - Robert, Jean Luc
AU - Martel, Cécile
AU - Veneziano, Rémi
AU - Henry, Céline
AU - El Dein, Ossama Sharaf
AU - Saint, Nathalie
AU - Brenner, Catherine
AU - Chopineau, Joel
N1 - Funding Information:
The work has been funded by l’Agence Nationale pour la Recherche (ANR-08PCVI-0008-01). CB laboratory is a member of the Laboratory of Excellence LERMIT supported by a grant from ANR (ANR-10-LABX-33). We are grateful to Martine Pugniere (PP2I platform at CRLC) for the access to the Biacore Instrument.
PY - 2012/12/7
Y1 - 2012/12/7
N2 - The voltage-dependent anion channel (VDAC) and the adenine nucleotide translocase (ANT) have central roles in mitochondrial functions such as nucleotides transport and cell death. The interaction between VDAC, an outer mitochondrial membrane protein and ANT, an inner membrane protein, was studied in isolated mitochondria and in vitro. Both proteins were isolated from various mitochondrial sources and reconstituted in vitro using a biomimetic system composed of recombinant human VDAC isoform 1 (rhVDAC1) immobilized on a surface plasmon resonance (SPR) sensor chip surface. Two enriched-preparations of HANT (ANT from heart, mainly ANT1) and LANT (ANT from liver, mainly ANT2) isoforms interacted differently with rhVDAC1. Moreover, the pharmacological ANT inhibitors atractyloside and bongkrekic acid modulated this interaction. Thus, ANT-VDAC interaction depends both on ANT isoform identity and on the conformation of ANT.
AB - The voltage-dependent anion channel (VDAC) and the adenine nucleotide translocase (ANT) have central roles in mitochondrial functions such as nucleotides transport and cell death. The interaction between VDAC, an outer mitochondrial membrane protein and ANT, an inner membrane protein, was studied in isolated mitochondria and in vitro. Both proteins were isolated from various mitochondrial sources and reconstituted in vitro using a biomimetic system composed of recombinant human VDAC isoform 1 (rhVDAC1) immobilized on a surface plasmon resonance (SPR) sensor chip surface. Two enriched-preparations of HANT (ANT from heart, mainly ANT1) and LANT (ANT from liver, mainly ANT2) isoforms interacted differently with rhVDAC1. Moreover, the pharmacological ANT inhibitors atractyloside and bongkrekic acid modulated this interaction. Thus, ANT-VDAC interaction depends both on ANT isoform identity and on the conformation of ANT.
KW - Channel
KW - Liposome
KW - Mitochondrion
KW - Surface plasmon resonance
UR - http://www.scopus.com/inward/record.url?scp=84870389816&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2012.10.108
DO - 10.1016/j.bbrc.2012.10.108
M3 - Article
C2 - 23131554
AN - SCOPUS:84870389816
SN - 0006-291X
VL - 429
SP - 12
EP - 17
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1-2
ER -