Abstract
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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Apoptosis / physiology
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COS Cells / metabolism
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Carrier Proteins / genetics
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Carrier Proteins / metabolism*
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Chlorocebus aethiops
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DNA, Complementary / genetics
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Endoplasmic Reticulum / metabolism*
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HeLa Cells
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Humans
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Intracellular Signaling Peptides and Proteins*
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Jurkat Cells / metabolism
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Membrane Proteins*
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Mitochondria / metabolism
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Molecular Sequence Data
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Myelin Proteins
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Nerve Tissue Proteins / genetics
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Nerve Tissue Proteins / metabolism
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Nogo Proteins
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Proto-Oncogene Proteins c-bcl-2 / metabolism*
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Sequence Homology, Amino Acid
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Subcellular Fractions / metabolism
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Translocation, Genetic
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bcl-X Protein
Substances
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BCL2L1 protein, human
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Carrier Proteins
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DNA, Complementary
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Intracellular Signaling Peptides and Proteins
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Membrane Proteins
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Myelin Proteins
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Nerve Tissue Proteins
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Nogo Proteins
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Proto-Oncogene Proteins c-bcl-2
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RTN1 protein, human
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RTN4 protein, human
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bcl-X Protein
Associated data
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GENBANK/AB040462
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GENBANK/AB040463