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. 2009 Mar 7;4(5):e5466. doi: 10.1371/journal.pone.0005466

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Lei et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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(A) The domain structure of MAVS. MAVS contains a N-terminal CARD-like domain, a C-terminal transmembrane domain (TM) and a central proline-rich region. The cartoon shows the structure of the three truncation mutants we used in the study. (B) The TM and CARD-like domains are not dispensable for the pro-apoptotic function of MAVS. 1 µg of wildtype MAVS and its three mutants depicted in (A) were introduced in HEK293T cells; and apoptosis was assessed by flow cytometry 48 h post-transfection using 7-AAD and Annexin V as markers of dead and apoptotic cells respectively. (C) The mitochondrial localization of MAVS is critical for its pro-apoptotic function. Cell viability was determined by XTT assay. (D) MAVS induces mitochondrial membrane potential collapse in HEK293T cells as quantified by TMRE staining. Each graph represents two separate experiments.