Functional and physical interaction between Bcl‐XL and a BH3‐like domain in Beclin‐1

@article{Maiuri2007FunctionalAP,
  title={Functional and physical interaction between Bcl‐XL and a BH3‐like domain in Beclin‐1},
  author={M. Maiuri and Ga{\"e}tane Le Toumelin and A. Criollo and J. Rain and F. Gautier and P. Juin and E. Tasdemir and G. Pierron and Kostoula Troulinaki and Nektarios Tavernarakis and J. Hickman and O. Geneste and G. Kroemer},
  journal={The EMBO Journal},
  year={2007},
  volume={26}
}
The anti‐apoptotic proteins Bcl‐2 and Bcl‐XL bind and inhibit Beclin‐1, an essential mediator of autophagy. Here, we demonstrate that this interaction involves a BH3 domain within Beclin‐1 (residues 114–123). The physical interaction between Beclin‐1 and Bcl‐XL is lost when the BH3 domain of Beclin‐1 or the BH3 receptor domain of Bcl‐XL is mutated. Mutation of the BH3 domain of Beclin‐1 or of the BH3 receptor domain of Bcl‐XL abolishes the Bcl‐XL‐mediated inhibition of autophagy triggered by… Expand
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