A novel protein, RTN-XS, interacts with both Bcl-XL and Bcl-2 on endoplasmic reticulum and reduces their anti-apoptotic activity.

Bcl-2 and Bcl-XL serve as critical inhibitors of apoptosis triggered by a broad range of stimuli, mainly acting on the mitochondria. We identified two members of the reticulon (RTN) family as Bcl-XL binding proteins, i.e., NSP-C (RTN1-C) and a new family member, RTN-XS, both of which did not belong to ...
the Bcl-2 family and were predominantly localized on the endoplasmic reticulum (ER). RTN-XS interacted with both Bcl-XL and Bcl-2, increased the localization of Bcl-XL and Bcl-2 on the ER, and reduced the anti-apoptotic activity of Bcl-XL and Bcl-2. On the other hand, NSP-C interacted only with Bcl-XL, affected the localization of Bcl-XL, and reduced Bcl-XL activity, but had no effect on Bcl-2. These results suggest that RTN family proteins can modulate the anti-apoptotic activity of Bcl-XL and Bcl-2 by binding with them and can change their localization to the ER.
Mesh Terms:
Amino Acid Sequence, Animals, Apoptosis, COS Cells, Carrier Proteins, Cercopithecus aethiops, DNA, Complementary, Endoplasmic Reticulum, Hela Cells, Humans, Intracellular Signaling Peptides and Proteins, Jurkat Cells, Membrane Proteins, Mitochondria, Molecular Sequence Data, Myelin Proteins, Nerve Tissue Proteins, Proto-Oncogene Proteins c-bcl-2, Sequence Homology, Amino Acid, Subcellular Fractions, Translocation, Genetic, bcl-X Protein
Oncogene
Date: Nov. 23, 2000
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