Mitochondrial membrane permeabilization by HIV-1 Vpr.

Article Details

Citation

Deniaud A, Brenner C, Kroemer G

Mitochondrial membrane permeabilization by HIV-1 Vpr.

Mitochondrion. 2004 Jul;4(2-3):223-33.

PubMed ID
16120388 [ View in PubMed
]
Abstract

The mitochondrion is a privileged target for apoptosis-modulatory proteins of viral origin. Thus, viral protein R (Vpr) can target mitochondria and induce apoptosis via a specific interaction with the permeability transition pore complex (PTPC). Vpr cooperates with the adenine nucleotide translocator (ANT) to form large conductance channels and to trigger all the hallmarks of mitochondrial membrane permeabilization (MMP). The Vpr/ANT interaction is direct, since it is abolished by the addition of a peptide corresponding to the Vpr binding site of ANT, ADP, ATP, or by Bcl-2. Accordingly, Vpr modulates MMP through direct structural and functional interactions with PTPC proteins.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
ADP/ATP translocase 1P12235Details
ADP/ATP translocase 3P12236Details
ADP/ATP translocase 2P05141Details