Maspin binds to cardiolipin in mitochondria and triggers apoptosis.

ABSTRACT: A central question in cell biology is how cells respond to stress signals and biochemically regulate apoptosis. One critical pathway involves the change of mitochondrial function and release of cytochrome c to initiate apoptosis. In response to apoptotic stimuli, we found that maspin-a noninhibitory member of the serine protease inhibitor superfamily-translocates from the cytosol to mitochondria and binds to cardiolipin in the inner mitochondrial membrane. Biolayer interferometry assay revealed that recombinant maspin binds cardiolipin with an apparent K_d,of ∼15.8 μM and competes with cytochrome c (apparent K_d of ∼1.31 μM) for binding to cardiolipin-enriched membranes. A hydrophobic, lysine-rich domain in maspin consists of 27 aa, is locate

SUBMITTER: Mahajan N 

PROVIDER: S-EPMC6463914 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature