Bax activates endophilin B1 oligomerization and lipid membrane vesiculation.

@article{Rostovtseva2009BaxAE,
  title={Bax activates endophilin B1 oligomerization and lipid membrane vesiculation.},
  author={Tatiana K. Rostovtseva and Hacene Boukari and Antonella Antignani and Brian B Shiu and Soojay Banerjee and Albert Neutzner and Richard J Youle},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 49},
  pages={34390-9}
}
Endophilins participate in membrane scission events that occur during endocytosis and intracellular organelle biogenesis through the combined activity of an N-terminal BAR domain that interacts with membranes and a C-terminal SH3 domain that mediates protein binding. Endophilin B1 (Endo B1) was identified to bind Bax, a Bcl-2 family member that promotes apoptosis, through yeast two-hybrid protein screens. Although Endo B1 does not bind Bax in healthy cells, during apoptosis, Endo B1 interacts… CONTINUE READING

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Highly Influenced

NUMBER 49 JOURNAL OF BIOLOGICAL CHEMISTRY 34399 at N anal Initutes of H ealth Lirary, on M arch

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Bax Activation of Endophilin B1/Bif-1 DECEMBER • 2002
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