BAX and BCL-XL can induce complementary Gaussian membrane curvatures to regulate apoptotic pore formation
نویسندگان
چکیده
Ghee Hwee Lai, Olena Ivashyna, Lori K. Sanders, Eric Christenson, Abhijit Mishra, Nathan W. Schmidt, Kiyotaka Akabori, Christian D. Santangelo, Paul H. Schlesinger, Gerard C. L. Wong Dept. of Bioengineering, Dept. of Chemistry, California NanoSystems Institute, University of California, Los Angeles, CA 90095 Dept. of Physics, Dept. of Materials Science and Engineering, University of Illinois, Urbana-Champaign, IL 61801 Dept. of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110 Dept. of Physics, University of Massachusetts, Amherst, MA 01003 Tel: 310-794-7684 E-mail: [email protected]
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Bax, but not Bcl-xL, decreases the lifetime of planar phospholipid bilayer membranes at subnanomolar concentrations.
Release of proteins through the outer mitochondrial membrane can be a critical step in apoptosis, and the localization of apoptosis-regulating Bcl-2 family members there suggests they control this process. We used planar phospholipid membranes to test the effect of full-length Bax and Bcl-xL synthesized in vitro and native Bax purified from bovine thymocytes. Instead of forming pores with repro...
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The Bcl-2 family of proteins, consisting of anti-apoptotic and pro-apoptotic members, regulates cell death by controlling mitochondrial membrane permeability that is crucial for apoptotic signal transduction. We have recently shown that some of these proteins, such as Bcl-x(L), Bax, and Bak, directly modulate the mitochondrial voltage-dependent anion channel (VDAC) and thus regulate apoptogenic...
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