Figure 5.

MOAP-1 cooperates with RASSF1A during death receptor-dependent apoptosis and promotes Bax activation. In response to death receptor stimulation, MOAP-1 is first recruited to the receptor and then followed by RASSF1A association at the MOAP-1/receptor complex. The association of MOAP-1 to RASSF1A promotes a conformational change in MOAP-1 that exposes its BH3-like domain required for Bax association. The subsequent interaction between MOAP-1 and Bax induces a conformational change in Bax that enables its translocation, and insertion into the mitochondrial outer membrane resulting in the release of cytochrome c and other apoptogenic factors, leading to apoptosis.