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            <title xml:lang="en">pRb/E2F-1-mediated caspase-dependent induction of Noxa amplifies the apoptotic effects of the Bcl-2/Bcl-xL inhibitor ABT-737</title>
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                <forename type="first">Joséphine</forename>
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            <idno type="halRefHtml">&lt;i&gt;Cell Death and Differentiation&lt;/i&gt;, 2013, 20 (5), pp.755 - 764. &lt;a target="_blank" href="https://dx.doi.org/10.1038/cdd.2013.6"&gt;&amp;#x27E8;10.1038/cdd.2013.6&amp;#x27E9;&lt;/a&gt;</idno>
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            <idno type="stamp" n="UNIV-ANGERS">Université d'Angers</idno>
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                <title xml:lang="en">pRb/E2F-1-mediated caspase-dependent induction of Noxa amplifies the apoptotic effects of the Bcl-2/Bcl-xL inhibitor ABT-737</title>
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                <title level="j">Cell Death and Differentiation</title>
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              <p>Although Bcl-2 family members control caspase activity by regulating mitochondrial permeability, caspases can, in turn, amplify the apoptotic process upstream of mitochondria by ill-characterized mechanisms. We herein show that treatment with a potent inhibitor of Bcl-2 and Bcl-xL, ABT-737, triggers caspase-dependent induction of the BH3-only protein, Mcl-1 inhibitor, Noxa. RNA interference experiments reveal that induction of Noxa, and subsequent cell death, rely not only on the transcription factor E2F-1 but also on its regulator pRb. In response to ABT-737, pRb is cleaved by caspases into a p68Rb form that still interacts with E2F-1. Moreover, pRb occupies the noxa promoter together with E2F-1, in a caspase-dependent manner upon ABT-737 treatment. Thus, caspases contribute to trigger the mitochondrial apoptotic pathway by coupling Bcl-2/Bcl-xL inhibition to that of Mcl-1, via the pRb/E2F-1-dependent induction of Noxa.</p>
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