International audienceThe proapoptotic protein Bak is implicated in the execution phase of apoptosis, a cell death program. Bak is essentially mitochondrial and during early steps of apoptosis undergoes conformational changes that lead to its full membrane integration in mitochondria and the subsequent liberation of pro-apoptotic mitochondrial proteins. Little is known about the partners and mechanisms implicated in the activation of Bak. We have recently shown that Bak is incorporated into a Voltage dependent anionic channel of type 2 (VDAC2)/Metaxin 1(Mtx1)/Metaxin 2 (Mtx2) multi-protein complex in both resting and dying cells. Here, we show that, after the induction of apoptosis, Bak switches from its association with Mtx2 and VDAC2 to a closer association with Mtx1. This change of partners is under the control of a tyrosine phosphorylation of Mtx1 by c-Abl
The proteins of the BCL-2 family (pBCL-2s) are involved in the sequence of events that culminates in apoptosis, a type I cell death program. The mitochondrion is the primary site of action of pBCL-2s and represents the cross roads between the initiation and the execution phases of apoptosis. pBCL-2s are either constitutively associated with the mitochondria outer membrane (MOM) or targeted to this membrane at the onset of apoptosis. The mechanisms implicated in their targeting and activation during apoptosis is largely unknown. Recently, several pBCL-2s have been shown to interact with components of the translocase of the outer membrane (TOM), a complex responsible for the import into and across the MOM of nuclear encoded mitochondrial proteins. Here we will review the available data and discuss the possible implications of this interaction in the apoptotic programme.
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