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. Author manuscript; available in PMC: 2009 May 6.
Published in final edited form as: Autophagy. 2008 Oct 14;4(7):949–951. doi: 10.4161/auto.6788

Figure 2. A speculative model of the interrelationship between the roles of JNK1-mediated Bcl-2 multi-site phosphorylation in autophagy regulation and apoptosis regulation.

Figure 2

According to this model, a low level of Bcl-2 multi-site phosphorylation occurs initially in response to starvation to promote cell survival by disrupting the Bcl-2/Beclin 1 complex (a lower affinity interaction) and activating autophagy. With prolonged starvation, higher levels of Bcl-2 multi-site phosphorylation leads to disruption of the the complex between Bcl-2/Bax (or other pro-apoptotic BH3 domain-containing proteins) (which are higher affinity interactions), promoting apoptosis at a time point when autophagy can no longer keep cells alive.