Modulator Of Apoptosis 1 (MOAP1)

MOAP1 was identified by its interaction with apoptosis regulator BAX protein. This protein contains a Bcl-2 homology 3 (BH3)-like motif, which is required for the association with BAX. When overexpressed, this gene has been shown to mediate caspase-dependent apoptosis.

MAP1 formed homodimers, and it associated with BAX, BCL2, and BCLXL (BCL2L1) in vitro and in transfected human embryonic kidney cells. MAP1 did not bind other members of the BCL2 family. Mutation analysis indicated that the BH3-like domain of MAP1 was required to mediate apoptosis and for binding of MAP1 to BAX, but not to BCLXL. All 3 BH domains of BAX were required for binding with MAP1.